"Life Without Bread"

Gertrudes said:
Laura said:
Gawan said:
Okay, with the protein restriction (started yesterday with about max 80 grams) something is definitely going on with my body, yesterday I felt almost the whole day very hungry, needed to to take a nap and ate only in the evening a little bit over the amount of proteins.

If you are feeling hungry, try eating a bit more fat. One thing I do is put a slice of butter on my plate and put a small chunk of it on every bite I eat just for the extra fat. If that doesn't do it, increase the protein. You may need more protein for various reasons. (And so may others.)

Laura said:
Makes me think that the overarching concept was that of the Odyssey: the suitors eating and drinking away Odysseus' goods and seeking to marry his wife. As we've seen in "The Odyssey" thread, the over-indulgence in food is associated with bringing on cataclysm. Over and over again, over-indulgence is highlighted as being a serious fault of character.

Makes sense. We can say that the same happens with sex. It's as if over indulgence of what is a primary need for our own, and our species survival, has been turned into a feel good buffer, and mostly a source of dependence and addiction. Not to mention that it is a huge money maker, and 2 of the things (if not THE 2 things) that are crippling and disabling people in ALL senses.
Just observing how much energy is invested in food (adverts, the number of existing diets and food theories, vegetarianism being but one of them) and sex (almost always an underlying theme in today's music, adverts, pretty much the whole of society's own image seems to have that background theme) one can only be baffled.
This isn't to say one shouldn't derive satisfaction from both food and sex, but simply not to loose one's way in it, and turn what is fuel or a means for species survival, into our main source of comfort or even our sole reason for existing.

Reminds me of the 7 Deadly Sins.

3.1 Lust
3.2 Gluttony
3.3 Greed
3.4 Sloth
3.4.1 Acedia
3.5 Wrath
3.6 Envy
3.7 Pride

Gluttony
http://en.wikipedia.org/wiki/Seven_deadly_sins

Derived from the Latin gluttire, meaning to gulp down or swallow, gluttony (Latin, gula) is the over-indulgence and over-consumption of anything to the point of waste. In the Christian religions, it is considered a sin because of the excessive desire for food or its withholding from the needy.[13]

Depending on the culture, it can be seen as either a vice or a sign of status. Where food is relatively scarce, being able to eat well might be something to take pride in. But in an area where food is routinely plentiful, it may be considered a sign of self-control to resist the temptation to over-indulge.

Medieval church leaders (e.g., Thomas Aquinas) took a more expansive view of gluttony,[13] arguing that it could also include an obsessive anticipation of meals, and the constant eating of delicacies and excessively costly foods.[14] Aquinas went so far as to prepare a list of six ways to commit gluttony, including:

Praepropere - eating too soon.

Laute - eating too expensively.

Nimis - eating too much.

Ardenter - eating too eagerly (burningly).

Studiose - eating too daintily (keenly).

Forente - eating wildly (boringly).
 

Attachments

  • Excess x Albert Anker,1896.jpg
    Excess x Albert Anker,1896.jpg
    102.6 KB · Views: 25
Laura said:
This is the canner I've got:
http://www.amazon.com/All-American-2-Quart-Pressure-Cooker-Canner/dp/B0002808ZM/ref=sr_1_16?s=home-garden&ie=UTF8&qid=1313086879&sr=1-16

Wow, you got the grandaddy Cadillac model! :D I can't afford $460 for a canner but fortunately there's lots more canners to choose from in the lower price ranges.

http://www.amazon.com/s/ref=nb_sb_ss_i_1_28?url=search-alias%3Dgarden&field-keywords=canners+and+pressure+cookers&sprefix=canners+and+pressure+cookers
 
Gertrudes said:
Laura said:
Gawan said:
Okay, with the protein restriction (started yesterday with about max 80 grams) something is definitely going on with my body, yesterday I felt almost the whole day very hungry, needed to to take a nap and ate only in the evening a little bit over the amount of proteins.

If you are feeling hungry, try eating a bit more fat. One thing I do is put a slice of butter on my plate and put a small chunk of it on every bite I eat just for the extra fat. If that doesn't do it, increase the protein. You may need more protein for various reasons. (And so may others.)

I think I'm one of those who needs a higher protein intake. Something similar happened to me Gawan, I cut down my protein intake yesterday and today to approach the upper limit of what I should supposedly be eating, and even though I ate more then my upper limit, I was starving today. This was definitely something not to repeat. I'm at my upper limit of fat intake, so upping it even more is out of the equation for now, I'm upping my vegetables but I'm also going to keep higher levels of protein since I feel that I do need them.

Everyone's metabolisms are different, adding to that, everyone's lifestyles are different. I was thinking of it today and with the amount of exercise I do there is no way I can get by with only a 40g of protein a day, so I think we'll have to keep experimenting, that is always bearing in mind that fat is unrestricted (according to personal tolerance), but not protein.

I was thinking about the 0.8 protein figure per Kg of body weight again today, and even though I read the quotes on protein, I am still struggling with this number, and here's why: assuming that our paleolithic ancestors ate nothing but meat and fat and very occasional sources of carbohydrates in the form of root vegetables and some fruits, for the figure of 0.8 per body weight kg, someone with my weight (around 44, 45kg) would have to eat only 36g of protein a day. I just weighted what I consider to be a small portion of stewed chicken (132g to be precise) that would give 36g of protein. This amount of food would in no way sustain a healthy individual for a whole day, even with plenty of added fat. Personally it wasn't enough for a single meal for me, even with the added fat and vegetables.
So all in all, I think we do need to do our own testing here.
Added: Maybe I'm missing something that's right under my nose and I'm just not seeing, happens often :/

Laura said:
Makes me think that the overarching concept was that of the Odyssey: the suitors eating and drinking away Odysseus' goods and seeking to marry his wife. As we've seen in "The Odyssey" thread, the over-indulgence in food is associated with bringing on cataclysm. Over and over again, over-indulgence is highlighted as being a serious fault of character.

Makes sense. We can say that the same happens with sex. It's as if over indulgence of what is a primary need for our own, and our species survival, has been turned into a feel good buffer, and mostly a source of dependence and addiction. Not to mention that it is a huge money maker, and 2 of the things (if not THE 2 things) that are crippling and disabling people in ALL senses.
Just observing how much energy is invested in food (adverts, the number of existing diets and food theories, vegetarianism being but one of them) and sex (almost always an underlying theme in today's music, adverts, pretty much the whole of society's own image seems to have that background theme) one can only be baffled.
This isn't to say one shouldn't derive satisfaction from both food and sex, but simply not to loose one's way in it, and turn what is fuel or a means for species survival, into our main source of comfort or even our sole reason for existing.

I'm with you on the too-little-protein-doesn't-work wagon. Yesterday and for breakfast and lunch today I reduced my protein intake. I tried to match 25 g per meal (which I know is more than the 68 g per day I should eat according to PBPM but you have to start somewhere :)) and was left hungry, unsatisfied, and I also recall having the same feeling that I had when I was doing a raw-food diet a couple of years ago where the body can't get warm and it's as if I can't get enough energy out into my limbs. I also lost the feeling of being energized and happy associated with the Atkins Edge.

After reading some posts about individual changes, I changes my dinner to eat until I felt full and one hour later, the Atkins Edge is back. I have noticed that my body is giving me a subtle signal that now is the time to stop eating. If I have even one more bite it's going to be too much. I've started to respect that little voice and it seems to work out.

I don't know if it is due to being one of the skinnies but I just need more protein - probably around 1.25 grams per kg of body weight. I am thinking that this may decrease as the body gets more used to burning fat and efficient in the energy distribution and utilization.
 
Laura said:
This is the canner I've got:
http://www.amazon.com/All-American-2-Quart-Pressure-Cooker-Canner/dp/B0002808ZM/ref=sr_1_16?s=home-garden&ie=UTF8&qid=1313086879&sr=1-16

(I was mistaken, it's 41 quarts, not 34).

Canning jars should be just ball jars with canning lids. (seal and screw top).

It is an All American model but when I looked to purchase the standard Ball jars some of the people commented on how they use those BPA lids.

http://www.amazon.com/gp/product/B000X1O8BI?ie=UTF8&force-full-site=1

The All American model I was looking at is here:

http://www.amazon.com/All-American-2-Quart-Pressure-Cooker-Canner/dp/B00004S893/ref=sr_1_2?s=kitchen&ie=UTF8&qid=1313089718&sr=1-2

It holds 7 quart jars just like some of the models right above it and its not too big to handle.


Edit: It appears there is another manufacturer that makes BPA free plastic lids. Their name is Tattler. So I suppose i can still order the Ball jars and just pay extra to get the BPA free lids as well but is it really any safer being plastic? And my other concern was if they would hold their seal as well as the metal ones.

http://www.amazon.com/Tattler-Reusable-Regular-Canning-Rubber/dp/B0051PDXCQ/ref=sr_1_1?s=home-garden&ie=UTF8&qid=1313100682&sr=1-1
 
Thor said:
I don't know if it is due to being one of the skinnies but I just need more protein - probably around 1.25 grams per kg of body weight. I am thinking that this may decrease as the body gets more used to burning fat and efficient in the energy distribution and utilization.

Also being one of the skinnies I was eating a lot of meat (300g-400g a day) - 75g-100g of protein a day. It seems I needed it at the time.
I've been noticing my intestines have been healing (due to the lessening of food allergies/inflammation in general), and as that's been happening my need for protein seems to have gradually reduced.

It possible that the body has a lot of repair/growth work to do, so needing a lot of protein may be required for a while. I'm pretty sure (and I'm in my 30's) that I've actually grown half an inch/an inch taller. I've gained a lot of muscle tone too.

I definitely needed to drop my protein intake though. On dropping to the 0.9g/0.8g per kg level I feel much better, so I must be back into regeneration/healing mode. I'm pretty sure a month ago I couldn't have survived on this small level of protein though.
 
Thor said:
Yesterday and for breakfast and lunch today I reduced my protein intake. I tried to match 25 g per meal (which I know is more than the 68 g per day I should eat according to PBPM but you have to start somewhere :)) and was left hungry, unsatisfied,

A few months ago, instead of cooking 2 eggs for my breakfast I started having 2 raw organic eggs (yolks unbroken, slurped down intact one by one) along with my bacon or sausage. Compared to when I would eat the same 2 eggs cooked, I find that I have a more 'full' feeling after eating them raw. Also, for me cooked eggs were harder to digest.

It may sound gross to eat them raw, but they really don't have a flavor and go down quite easily. It enabled me to take in less protein and still feel full. From some research I've done, when eggs are exposed to heat the proteins and fats contained in the eggs are altered in a form that is not very beneficial for the body. When cooked, the protein of the egg undergoes a change in its chemical shape. It is mostly because of the cooking process that eating eggs results in some kind of allergies. Generally, consumption of raw eggs does not cause any kind of allergy. As well, they are easier to digest when in their raw state.

I'll find the information on eating them raw and post back.
 
The Chemistry of Amino Acids
http://www.biology.arizona.edu/biochemistry/problem_sets/aa/aa.html

Amino acids play central roles both as building blocks of proteins and as intermediates in metabolism. The 20 amino acids that are found within proteins convey a vast array of chemical versatility. The precise amino acid content, and the sequence of those amino acids, of a specific protein, is determined by the sequence of the bases in the gene that encodes that protein. The chemical properties of the amino acids of proteins determine the biological activity of the protein. Proteins not only catalyze all (or most) of the reactions in living cells, they control virtually all cellular process. In addition, proteins contain within their amino acid sequences the necessary information to determine how that protein will fold into a three dimensional structure, and the stability of the resulting structure. The field of protein folding and stability has been a critically important area of research for years, and remains today one of the great unsolved mysteries. It is, however, being actively investigated, and progress is being made every day.

As we learn about amino acids, it is important to keep in mind that one of the more important reasons to understand amino acid structure and properties is to be able to understand protein structure and properties. We will see that the vastly complex characteristics of even a small, relatively simple, protein are a composite of the properties of the amino acids which comprise the protein.

Essential amino acids

Humans can produce 10 of the 20 amino acids. The others must be supplied in the food. Failure to obtain enough of even 1 of the 10 essential amino acids, those that we cannot make, results in degradation of the body's proteins—muscle and so forth—to obtain the one amino acid that is needed. Unlike fat and starch, the human body does not store excess amino acids for later use—the amino acids must be in the food every day.

The 10 amino acids that we can produce are alanine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine and tyrosine. Tyrosine is produced from phenylalanine, so if the diet is deficient in phenylalanine, tyrosine will be required as well. The essential amino acids are arginine (required for the young, but not for adults), histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. These amino acids are required in the diet. Plants, of course, must be able to make all the amino acids. Humans, on the other hand, do not have all the the enzymes required for the biosynthesis of all of the amino acids.

Why learn these structures and properties?
It is critical that all students of the life sciences know well the structure and chemistry of the amino acids and other building blocks of biological molecules. Otherwise, it is impossible to think or talk sensibly about proteins and enzymes, or the nucleic acids.

Amino Acids

Alanine
http://en.wikipedia.org/wiki/Alanine

Alanine is a nonessential amino acid, meaning it can be manufactured by the human body, and does not need to be obtained directly through the diet. Alanine is found in a wide variety of foods, but is particularly concentrated in meats.
Good sources of alanine include
Animal sources: meat, seafood, caseinate, dairy products, eggs, fish, gelatin, lactalbumin
Vegetarian sources: beans, nuts, seeds, soy, whey, brewer's yeast, brown rice, bran, corn, legumes, whole grains.

Arginine
http://fr.wikipedia.org/wiki/Arginine

Arginine is an amino acid "semi-essential" normally synthesized by the body according to his needs, from which the body produces nitric oxide (a substance that promotes blood vessel dilation) and creatine ( non-essential nutrient involved in the development and functioning of the muscles).
Arginine acts on erectile dysfunction (because nitric oxide helps the blood flow). It does not improve sexual function in subjects with no problems.
Arginine combined with other amino acids (ornithine), has an effect on the secretion of growth hormones, the rate of muscle mass and strength but then arginine alone has no effect on physical performance. Thus, combined with zinc, it allows the testicles to produce sperm most abundant, testicles swelling up to 50% (1.5 x) in some individuals.
Arginine is found in brown rice, oats and buckwheat, as well as red meat, poultry, fish, dairy products, nuts and wine.
An external supply of arginine is required only after a major trauma, severe infection, a major surgery.
Is not considered an essential nutrient, no recommended dietary allowance has been established for arginine.

Asparagine
http://fr.wikipedia.org/wiki/Asparagine

Asparagine was the first amino acid discovered in 1806 by Louis-Nicolas Vauquelin who was studying the asparagus , hence its name.
We often associate the odor of urine after eating asparagus asparagine, but some scientists disagree and implicate other substances such as methanethiol.

Aspartic acid
http://en.wikipedia.org/wiki/Aspartic_acid

Aspartic acid is not an essential amino acid, which means that it can be synthesized from central metabolic pathway intermediates in humans. Aspartic acid is found in:
Animal sources: luncheon meats, sausage meat, wild game
Vegetable sources: sprouting seeds, oat flakes, avocado, asparagus[citation needed], young sugarcane, and molasses from sugar beets.[1]
Dietary supplements, either as aspartic acid itself or salts (such as magnesium aspartate)
The sweetener aspartame (NutraSweet, Equal, Canderel, etc.)

Cysteine
http://fr.wikipedia.org/wiki/Cyst%C3%A9ine

Cysteine ​​involved in the synthesis of melanin , the natural pigment of the skin and hair.
Sources:
yeast
wheat germ
garlic
onion
Brussels sprouts
broccoli
dairy
nuts
seeds
Seafood
fish
eggs
meat

Glutamine
http://fr.wikipedia.org/wiki/Glutamine

Nutrition:
Because it can be synthesized from glutamic acid, glutamine is not an essential amino acid .
Glutamine serves as a supplement in the diet of frequent weight, and as a treatment for muscle cramps in the elderly. It provides among others a better recovery during physical effort (strength sports, etc. ..) and helps rebuild damaged muscle tissue. It also prevents the syndrome of overtraining 3 .

Currently, studies are still conducted on the potential adverse consequences of excessive absorption of glutamine, again without results. And its consumption is healthy because it can supposedly be used to fill the reserves of amino acids a session of physical exercise could have been empty. This is why it is often prescribed to people who are fasting, or suffering from physical trauma, a defective immune system or cancer.

In addition, recent studies have been conducted to better understand the effects and properties of glutamine, and these show a link between a diet rich in glutamine and beneficial effects on the intestines. Glutamine would include improving the maintenance functions of the intestinal wall , proliferation of the intestinal flora , as well as cell differentiation and a reduction in infections. It seems that these properties are due to an extraction rate of glutamine higher than that of other amino acids, which would make the best choice for the improvement of the bowel 4 .

These results were discovered after comparing plasma concentration in the intestines between diets high and low in glutamine. Yet although it seems that glutamine has properties "cleaning" is not clear to what extent it would have therapeutic benefits due to large variations in glutamine concentration in food 4 .

In addition, glutamine is known for its various effects on the acceleration of healing after surgery. The recovery time after abdominal surgery are reduced if the patient is fed intravenously with mixtures containing glutamine. Clinical trials seem to have shown that patients undergoing this type of plan, compared with those who had no glutamine, present including improved nitrogen balance, improved generation of cysteinyl- leukotrienes from granulocytes , a improve the restoration of leukocytes and intestinal permeability, all without side effects apparent.

Glycine
http://fr.wikipedia.org/wiki/Glycine_(acide_amin%C3%A9)

The glycine molecule acts as a neurotransmitter inhibitor at the spinal cord.

Glycine is a precursor of porphyrins, but also of creatine (in the liver ), the uric acid (a form of excretion of ammonia in birds ), of glutathione (a compound which participates in the reduction of free radicals ).

It is a component of bile acids primary: it combines with bile salts , making them more soluble.

Added to the succinyl-CoA it forms the heme of the hemoglobin , for example.

It s'interconvertit with serine and threonine , and is the final molecule of the degradation of choline:
serine + tetrahydrofolate 5,10-methylenetetrahydrofolate + glycine + H 2 O.

Between glycine in the synthesis of glutathione

Histidine
http://fr.wikipedia.org/wiki/Histidine

Histidine is an amino acid that fulfills important functions in the structure and function of proteins . The imidazole ring of histidine has an atom of nitrogen that can capture a proton with a pKa close to neutral (pKa ~ 6.8) and therefore under physiological conditions. This property is crucial for the function of proteins:

It allows certain histidine residues present in the active sites of enzymes involved in reactions of proton transfer in the physiological conditions of the cytoplasm ( pH ~ 7).

In the hemoglobin , the histidines present in the protein involved in maintaining the pH of blood, acting as a molecule buffer.

The nitrogen of the imidazole ring of histidine can also form links of coordination with metal ions such as Zn 2 + , Co 2 + , Fe 2 + or Ni 2 + . These connections are important for the binding of these ions in metalloproteins , where the complexation of the metal is required for the activity of the protein. Examples include a histidine as axial ligand of iron in myoglobin and the hemoglobin and two histidines in the complexation of zinc present in the collagenase, a protease that degrades collagen.

Isoleucine
http://fr.wikipedia.org/wiki/Isoleucine

Biochemistry
It has a second asymmetric carbon in addition to carbon α and only the form 2S-3S is found in nature. The proportion of isoleucine in the protein human is about 4.6%.

Leucine
http://fr.wikipedia.org/wiki/Leucine

The leucine (C 6 H 13 NO 2 ), branched amino acid (essential) non-polar, higher homologue of valine, is the most common 20 amino acids . Its name in systematic nomenclature is 2-Amino-4-methylpentanoic. Its chemical composition is identical to that of isoleucine , but its atoms are arranged differently, which gives it different properties. From the perspective of nutrition , leucine is in humans, an essential amino acid . It is found in significant amounts in wheat germ ( 2170 mg ), tuna ( 2170 mg ), peanuts ( 2050 mg ), salmon ( 1770 mg ), beef tenderloin ( 1700 mg ) , chickpeas ( 1460 mg ), cottage cheese (curd 1 230 mg ) and rice (full 690 mg ). According to an article by researchers at the INRA in the Journal of Physiology December 2005, the addition of leucine in the diet of rats would allow regulation of the "nitrogen balance". This altered during aging, causing an imbalance between production and degradation of muscle proteins. This is the origin of the muscle loss observed in the elderly. It remains to show that the results obtained with rats are reproducible with the human species before considering a supplemental leucine in the diet of the elderly.

Lysine
http://fr.wikipedia.org/wiki/Lysine

The peptide poly-lysine is a polymer of several lysines. Since the amine group has a pK a of 10.2, this group is positively charged (-NH 3 + ) at pH (neutral) 7.
With the positively charged polymer, DNA can be linked (in the construction of micro-arrays of DNA at neutral pH (and basic), a surface of glass is negatively charged groups in SiO - . They may have electrostatic bonds with polylysine, which in turn binds to the negative groups of phosphate of DNA.

Methionine
http://fr.wikipedia.org/wiki/Methionine

Biological roles
Methionine plays a special role in protein biosynthesis , since all protein chains start with the incorporation of a methionine N-terminal position. Other methionine residues can then be incorporated internally to the chain polypeptides. The first methionine of the protein is not always found in proteins over. Indeed, it is frequently cleaved by a specific enzyme called methionine aminopeptidase.

Methionine is also a transmethylase, it has the ability to transfer the methyl group bound to sulfur. Also the breaking of this bond releases a large amount of energy.

Also, it is used as an antidote to paracetamol 100 mg of methionine per 500 mg of paracetamol

Phenylalanine
http://fr.wikipedia.org/wiki/Phenylalanine

The phenylalanine is an amino acid aromatic non- polar which are derived, in particular, the tyrosine and the aspartame . Its core benzene gives an absorption spectrum especially in the UV around 260 nm wavelength. It comes in the form of two enantiomers due to the chirality of the atom of carbon bearing the amine and acid. In humans, it is an essential amino acid that is to say, it must be provided by the diet because the body is unable to synthesize.

Medical
Phenylalanine is present especially in chewing gum , if this molecule has no effect in the proportion of gum to see two or more per day, it will have a laxative effect against in higher quantity (or even 2 3 packets of chewing gum per day), because the action of phenylalanine in the body in large doses is an accelerating intestinal transit.

Of phenylalanine found in most common foods

Cereals and cereal products
Starchy roots, tubers
Legumes and derived products
Nuts and seeds
Vegetables
Fruits
Meat and poultry
Eggs
Fish , crustaceans , molluscs and fish products
Milk and dairy products
Yeasts and algae
Seeds and vegetables are the foods most of phenylalanine, closely followed by some cheese (especially dry).

Proline
http://fr.wikipedia.org/wiki/Proline

L- proline or proline by abuse of language, is one of 20 amino acids of the genetic code . In human proteins, its frequency is 5.2%.
L- proline ( enantiomer of absolute configuration S) is also used to living organisms to assemble proteins. This is known as amino acids proteinogenic .

Proline may act by breaking the α helices because it can form hydrogen bond (due to its secondary amine) and therefore destabilizes the α helix, or form a junction in the β sheets . The presence of many prolines can cause a propeller to proline (as is the case of collagen ). Proline has a function amine secondary and not a function imine (The error is present in some French-language works of Biochemistry. But let us not forget that the chemistry and biochemistry are never at odds vocabulary for chemical functions).

Proline participates mainly collagen synthesis and wound healing.

Serine
http://en.wikipedia.org/wiki/Serine

Biological function: Metabolic
Serine is important in metabolism in that it participates in the biosynthesis of purines and pyrimidines. It is the precursor to several amino acids including glycine and cysteine, and tryptophan in bacteria. It is also the precursor to numerous other metabolites, including sphingolipids and folate, which is the principal donor of one-carbon fragments in biosynthesis.

Signaling
D-Serine, synthesized in the brain by serine racemase from L-serine (its enantiomer), serves as both a neurotransmitter and a gliotransmitter by activating NMDA receptors, making them able to open if they then also bind glutamate. D-serine is a potent agonist at the glycine site of the NMDA-type glutamate receptor. For the receptor to open, glutamate and either glycine or D-serine must bind to it. In fact, D-serine is a more potent agonist at the glycine site on the NMDAR than glycine itself. D-serine was only thought to exist in bacteria until relatively recently; it was the second D amino acid discovered to naturally exist in humans, present as a signalling molecule in the brain, soon after the discovery of D-aspartate. Had D amino acids been discovered in humans sooner, the glycine site on the NMDA receptor might instead be named the D-serine site

Threonine
http://en.wikipedia.org/wiki/Threonine

Biosynthesis
As an essential amino acid, threonine is not synthesized in humans, hence we must ingest threonine in the form of threonine-containing proteins. In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. Homoserine undergoes O-phosphorylation; this phosphate ester undergoes hydrolysis concomitant with relocation of the OH group.[3] Enzymes involved in a typical biosynthesis of threonine include:

1. aspartokinase
2. ß-aspartate semialdehyde dehydrogenase
3. homoserine dehydrogenase
4. homoserine kinase
5. threonine synthase.

Tryptophan
http://en.wikipedia.org/wiki/Tryptophan

Tryptophan (IUPAC-IUBMB abbreviation: Trp or W; IUPAC abbreviation: L-Trp or D-Trp; sold for medical use as Tryptan)[2] is one of the 20 standard amino acids, as well as an essential amino acid in the human diet. It is encoded in the standard genetic code as the codon UGG. The slight mispronunciation "tWiptophan" can be used as a mnemonic for its single letter IUPAC code W.[3] Only the L-stereoisomer of tryptophan is used in structural or enzyme proteins, but the D-stereoisomer is occasionally found in naturally produced peptides (for example, the marine venom peptide contryphan).[4] The distinguishing structural characteristic of tryptophan is that it contains an indole functional group. It is an essential amino acid as demonstrated by its growth effects on rats

Tyrosine
http://en.wikipedia.org/wiki/Tyrosine

Tyrosine (abbreviated as Tyr or Y)[1] or 4-hydroxyphenylalanine, is one of the 20 amino acids that are used by cells to synthesize proteins. Its codons are UAC and UAU. It is a non-essential amino acid with a polar side group. The word "tyrosine" is from the Greek tyri, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese.[2][3] It is called tyrosyl when referred to as a functional group or side chain.

Functions
Aside from being a proteogenic amino acid, tyrosine has a special role by virtue of the phenol functionality. It occurs in proteins that are part of signal transduction processes. It functions as a receiver of phosphate groups that are transferred by way of protein kinases (so-called receptor tyrosine kinases). Phosphorylation of the hydroxyl group changes the activity of the target protein.

A tyrosine residue also plays an important role in photosynthesis. In chloroplasts (photosystem II), it acts as an electron donor in the reduction of oxidized chlorophyll. In this process, it undergoes deprotonation of its phenolic OH-group. This radical is subsequently reduced in the photosystem II by the four core manganese clusters.

Dietary sources
Tyrosine, which can also be synthesized in the body from phenylalanine, is found in many high protein food products such as soy products, chicken, turkey, fish, peanuts, almonds, avocados, milk, cheese, yogurt, cottage cheese, lima beans, pumpkin seeds, and sesame seeds.[4] Tyrosine can also be obtained through supplementation.

Valine
http://en.wikipedia.org/wiki/Valine

Valine (abbreviated as Val or V)[3] is an α-amino acid with the chemical formula HO2CCH(NH2)CH(CH3)2. L-Valine is one of 20 proteinogenic amino acids. Its codons are GUU, GUC, GUA, and GUG. This essential amino acid is classified as nonpolar. Human dietary sources include cottage cheese, fish, poultry, peanuts, sesame seeds, and lentils.

Along with leucine and isoleucine, valine is a branched-chain amino acid. It is named after the plant valerian. In sickle-cell disease, valine substitutes for the hydrophilic amino acid glutamic acid in hemoglobin. Because valine is hydrophobic, the hemoglobin does not fold correctly.

Atoms in Amino Acids
Hydrogen
Carbon
nitrogen
Oygen
Sulfur

Amino Acids & Bodybuilding
http://getbig.com/articles/protein.htm
 
This is day 2 of protein restriction of 0.9g/kg/day protein. (I'm 75 kilos, yielding 67g of protein daily). What I ate today:

80g sardines with olive oil (25g protein)
2 eggs with 2 slices serrano ham and a lot of butter (25 g protein)
100g shrimps fried in butter and some fat-only bacon (20g protein)

Although I'm not hungry, my legs are feeling rather weak again and the Ketostix indicate the highest value ever: 16 mmol/L. I even was feeling the ketones in my lungs -- it feels almost like acetone solvent -- wanting to breathe them out. I drunk more water and the feeling receded. Ketones are water soluble and go into the urine too.

I mentioned a few days ago that I was in ketosis and felt the "Atkins edge". But I'm not so sure any more. If I had been in ketosis, I would't feel so weak now. So my new theory is: When I felt well again after reducing the carbs, this was not ketosis or Atkins Edge, but simply the adaption to gluconeogenesis. NOW that I even restrict the gluconeogenesis, there is the crisis again, but it is also a chance to get into ketosis. Not sure if I'm right but it sounds kinda logical.

Thor said:
I don't know if it is due to being one of the skinnies but I just need more protein - probably around 1.25 grams per kg of body weight. I am thinking that this may decrease as the body gets more used to burning fat and efficient in the energy distribution and utilization.

Maybe that just keeps your gluconeogenesis which prevents you from real ketosis and the real Atkins Edge? I'm not sure if I have attained it, I'm just speculating.
 
Black Swan said:
Wow, you got the grandaddy Cadillac model! :D I can't afford $460 for a canner but fortunately there's lots more canners to choose from in the lower price ranges.

http://www.amazon.com/s/ref=nb_sb_ss_i_1_28?url=search-alias%3Dgarden&field-keywords=canners+and+pressure+cookers&sprefix=canners+and+pressure+cookers

Yes. I've got a big family to feed and it is way more efficient to do the canning in larger batches. It DOES take about 20 minutes to get up the steam and 90 minutes to process, and over an hour to cool down, so it's not like you can really do more than one batch a day unless you do nothing else!

We get stew beef with plenty of fat on it for about 1.74 euro per pound, so it is really a good deal. We tried one of the jars of meat for supper one night, and even if it goes in tough, it comes out melt-in-your-mouth tender!
 
Thor said:
I think I'm one of those who needs a higher protein intake. Something similar happened to me Gawan, I cut down my protein intake yesterday and today to approach the upper limit of what I should supposedly be eating, and even though I ate more then my upper limit, I was starving today. This was definitely something not to repeat. I'm at my upper limit of fat intake, so upping it even more is out of the equation for now, I'm upping my vegetables but I'm also going to keep higher levels of protein since I feel that I do need them.

Yes, you may need to do this for awhile until your gut heals. If you work at it with supplementation, you can accomplish it in a year or less, but otherwise, it can take years. Once your gut is healed, it will process what you eat with more efficiency and you may be able to reduce your intake without feeling hunger. In fact, you may reduce it naturally.

Now that I've said that, I think that is how it ought to happen: it should be natural.

But the important things are these: 1) the attention on gut healing is crucial; 2) we now know that there is a way to possibly reverse severe damage in the rest of the body once the gut is healed and nutrition is restored.


RedFox said:
Also being one of the skinnies I was eating a lot of meat (300g-400g a day) - 75g-100g of protein a day. It seems I needed it at the time.
I've been noticing my intestines have been healing (due to the lessening of food allergies/inflammation in general), and as that's been happening my need for protein seems to have gradually reduced.

Yes, that seems to be where a few of us are getting. It does feel pretty good to be able to take some foods back that were impossible to eat before plus feeling like you are getting real nourishment from much less food.

RedFox said:
It possible that the body has a lot of repair/growth work to do, so needing a lot of protein may be required for a while. I'm pretty sure (and I'm in my 30's) that I've actually grown half an inch/an inch taller. I've gained a lot of muscle tone too.

I definitely needed to drop my protein intake though. On dropping to the 0.9g/0.8g per kg level I feel much better, so I must be back into regeneration/healing mode. I'm pretty sure a month ago I couldn't have survived on this small level of protein though.

Yup, same here. I think that, in the beginning, you just have to eat a lot of meat/fat and even some non-aggravating veggies for the duration, until the gut really begins to heal.

Data said:
This is day 2 of protein restriction of 0.9g/kg/day protein. (I'm 75 kilos, yielding 67g of protein daily).

Although I'm not hungry, my legs are feeling rather weak again and the Ketostix indicate the highest value ever: 16 mmol/L. I even was feeling the ketones in my lungs -- it feels almost like acetone solvent -- wanting to breathe them out. I drunk more water and the feeling receded. Ketones are water soluble and go into the urine too.

I mentioned a few days ago that I was in ketosis and felt the "Atkins edge". But I'm not so sure any more. If I had been in ketosis, I would't feel so weak now. So my new theory is: When I felt well again after reducing the carbs, this was not ketosis or Atkins Edge, but simply the adaption to gluconeogenesis. NOW that I even restrict the gluconeogenesis, there is the crisis again, but it is also a chance to get into ketosis. Not sure if I'm right but it sounds kinda logical.

Yes, it does. But maybe you should up the protein just a tad? Like everyone, I think you need some gut-healing time.

Again, Psyche mentioned Boswellia - do take advantage of this truly effective supplement that reduces inflammation especially in the gut. Atriedes took it regularly after getting out of the hospital, along with his L-Glutamine and colostrum/lactoferrin. I've taken it a few times myself and it is pretty effective on inflammation in general. Funny that all the best supplements come from trees...
 
I have been doing the low carb diet for about a week and a half now and I must say, I am really starting to feel amazing!!! The first few days my head hurt, I felt lethargic, and my legs felt so heavy. But after I got past that, I have so much energy. I don't get tired anymore around 3pm. The best part is, I am not constantly thinking and obsessing about food. I feel a real sense of inner calm. My skin looks better, my hair looks better too.
I have been having bacon and eggs for breakfast, a pork chop or other piece of meat for lunch, and usually some pork and sometimes some green beans for dinner. I still have been having a slight headache daily, but it seems to be getting better and better.
I have also lost some weight! Woo hoo!!!
 
On my second day at 63.5g protein (right for my weight), and I'm a skinny too, and the energy is flowing still. Carbs have dropped from approx 20g to approx 15g too. No empty tummy feeling today, no cravings, eat when feel the need (and to fit in with other activities out of house). Adding a slice of butter with each meal helps too.
 
brainwave said:
But I will focus on healing the gut first and foremost. I am much more motivated when I have something I can work on immediately.

Makes sense. :)

I wonder if now would be a good time to make bone broth? Might be good for your bronchitis, it's got that 'grandma's good, nurturing feel' and it has an incredibly long list of benefits for imbalances some of which are:

allergies
anemia
anxiety
asthma
carbohydrate maldigestion
Celiac Disease
depression
detoxification
Diabetes
diarrhea
fatigue
food sensitivities
immunodepression
infectious disease
inflammation
Inflammatory Bowel Disease (Crohn's Disease and Ulcerative Colitis)
irritability
Irritable Bowel Syndrome
leaky gut
loss of appetite
meat maldigestion
muscle cramps
muscle spasms
nausea
pain

Basic Broth Making and Usage
Ingredients

1. Bones - from poultry, fish, shellfish, beef, lamb*
cooked remnants of a previous meal, with or without skin and meat

raw bones, with or without skin and meat**

use a whole carcass or just parts (good choices include feet, ribs, necks and knuckles)

don't forget shellfish shells, whole fish carcasses (with heads) or small dried shrimp
2. Water - start with cold water
enough to just cover the bones

or 2 cups water per 1 pound bones
3. Vinegar - apple cider, red or white wine, rice, balsamic
a splash

2 tablespoons per 1 quart water or 2 pounds bones

lemon juice may be substituted for vinegar (citric acid instead of acetic acid)
4. Vegetables (optional) - peelings and scraps like ends, tops and skins or entire vegetable
celery, carrots, onions, garlic and parsley are the most traditionally used, but any will do

if added towards the end of cooking, mineral content will be higher
Recipe

Combine bones, water and vinegar in a pot, let stand for 30 minutes to 1 hour, bring to a simmer, remove any scum that has risen to the top, reduce heat and simmer (6 - 48 hrs for chicken, 12 - 72 hrs for beef). To reduce cooking time, you may smash or cut bones into small pieces first. If desired, add vegetables in last ½ hour of cooking (or at any point as convenience dictates). Strain through a colander or sieve, lined with cheesecloth for a clearer broth. Discard the bones. If uncooked meat was used to start with, reserve the meat for soup or salads.

An easy way to cook broth is to use a crockpot on low setting. After putting the ingredients into the pot and turning it on, you can just walk away. If you forget to skim the impurities off, it's ok, it just tastes better if you do. If you wish to remove the fat for use in gravy, use a gravy separator while the broth is warm, or skim the fat off the top once refrigerated. Cold broth will gel when sufficient gelatin is present. Broth may be frozen for months or kept in the refrigerator for about 5 days.

Usage

1. Soup - Make soup by adding vegetables, beans, grains or meat to broth. Briefly cook vegetables and meat with butter or oil in the bottom of a stockpot (5 minutes). Add broth, and grains or previously soaked beans if you wish. Simmer until everything is cooked through. Time will vary with the ingredients used, but count on a minimum of 20 minutes. Season at the end of cooking with salt and pepper and spices of your choice. Consult cookbooks for specific recipe ideas.

2. Cooking Liquid - Use broth in place of water to cook rice, beans or other grains. Bring broth to a boil, add grains or beans, reduce heat and cook for instructed time. Or you can simmer vegetables or meat in a little seasoned broth until cooked. Remove to a plate, thicken broth with cornstarch, arrowroot or flour, then pour over vegetables and meat.

3. Gravy - Make gravy to put on vegetables, meat or biscuits. Put fat (removed from the broth, or use butter) in a skillet. Add any type of flour, 1 tablespoon at a time, and stir constantly until browned. Whisk in broth and cook till thickened. Add salt and pepper to taste.

4. Tea - Don't forget you can just add salt and sip broth like tea. This is especially nice in the winter or if you're feeling sick. Since broth is simultaneously energizing and calming, it can take the place of morning coffee, afternoon tea, or evening nightcap. Try it in a thermos and sip throughout the day. Of course, the most traditional use for seasoned broth is as a first course, to enhance the digestion of any meal to come.

*Pork bones are not generally recommended for prepared ahead broth, but are cooked into stew and soup recipes, and boiled pig skin is traditionally consumed for many of the same purposes as broth.
**Raw bones and meat may be browned first in the oven, or in the bottom of the stockpot to enhance flavor and color.

The full article is here: http://www.sott.net/articles/show/232028-Traditional-Bone-Broth-in-Modern-Health-and-Disease
 
1984 said:
A few months ago, instead of cooking 2 eggs for my breakfast I started having 2 raw organic eggs (yolks unbroken, slurped down intact one by one) along with my bacon or sausage. Compared to when I would eat the same 2 eggs cooked, I find that I have a more 'full' feeling after eating them raw. Also, for me cooked eggs were harder to digest.

It may sound gross to eat them raw, but they really don't have a flavor and go down quite easily. It enabled me to take in less protein and still feel full. From some research I've done, when eggs are exposed to heat the proteins and fats contained in the eggs are altered in a form that is not very beneficial for the body. When cooked, the protein of the egg undergoes a change in its chemical shape. It is mostly because of the cooking process that eating eggs results in some kind of allergies. Generally, consumption of raw eggs does not cause any kind of allergy. As well, they are easier to digest when in their raw state.

I'll find the information on eating them raw and post back.

That is interesting to hear 1984. I have recently begun to play with raw meat. I'm still very cautious (especially because of bacteria or parasites) but I'm finding that it fills me up more than cooked meat. I'm eating thin slices or small cubes. I tried to put some condiments on it but the best taste was just pure red raw meat. Although salt sometimes is nice.

I've been researching the benefits of raw meat but I did not find good scientific data yet. I'll post here as soon as I do. Meanwhile there are some raw paleo forums and a guy called Aajonus Vonderplanitz who apparently eats only raw meat and some raw vegetables. They all speak wonders of eating raw meat. I thought it might be one way of dealing with some of the difficulties of digesting meat and fat, as raw meat seems to have enzymes that are degraded when cooked.
 
I finally got the books, Vegetarian Myth, Life with out Bread and Low Carbohydrate living. Also got a decent copy of Planet X, Comets and Earth Changes. This was the slowest service I've ever had from Amazon.

Starting Monday I begin 7 days off from work. I have some home projects to do, but most of the time will be spent studying and being out in quiet natural places.

I started VM. Already legions of long held beliefs and assumptions are being vaporized. The lies that are fed to us from childhood on are awesome and vile.

My real education continues.

Mac
 
Back
Top Bottom