Histidine consumption prior to prolonged aerobic exercise as a method to increase myoglobin production potential

I was able to, with difficulty, find information regarding: the molecular weight of specicic amino acids in the human body as a percent of the total molecular weight of amino acids in the human body ( http://www.jadenutra.com/aminoacids.html); the composition of human myoglobin (http://www.aw-bc.com/mathews/ch07/c07emhp.htm, http://www.aw-bc.com/mathews/ch05/fi5p14.htm, the molecular weight of the various proteins that compose human myoglobin (http://www.webqc.org/aminoacids.php).

Thus I was by extrapolation able to estimate the difference between an amino acid's percent of total molecular weight in the human body in general compared to an amino acid's percent of total molecular weight in myoglobin. The idea being that the more the latter exceeds the former, the more the amino acids should be emphasized for consumption prior to prolonged aerobic exercise.

I found that certain amino acids comprise a higher percentage of the total molecular weight of myoglobin, compared to their percentage of the total molecular weight of amino acids in the human body.

My estimates (% of molecular weight of myoglobin, % of molecular weight of amino acids in body in general, the first stat divided by the second to produce a ratio for the third stat, the third ratio stat multiplied times the first stat to produce the fourth stat):

Table 1:

glutamate 10.4, 6.2, 1.7, 17.7; histidine 7.2, 2.1, 3.4, 24.5; tryptophan, 2.0, 1.1, 1.8, 3.6; lysine 14.9, 7.0, 2.1, 31.3.

The fourth stat in table 1 is an attempt to measure an amino acid's importance at a time when the intent is to increase myoglobin production potential in the body (at such a time amino acids that are especially important for myoglobin production should be prioritized).

The fourth stat in Table 1 is the highest for lysine (31.3), and the second highest for histidine (24.5).

Using the method used in the previous post of comparing ('essential' amino acids only) an amino acid's percentage of total pieces of amino acids in myoglobin, to percent of total mg per kg body weight requirements, the figures for histidine are 12% and 6% a ratio of 2.0 (third stat in table 1). The 2.0 ratio figure times 12% = 24 (fourth stat in table 1) as an indicator of importance for timely production of myoglobin specifically, which is almost the same as the 24.5 figure for 'the fourth stat' for histidine derived from the method used today.

In the previous post (http://davidvirgil.blogspot.com/2009/06/myoglobin-used-by-body-during-prolonged.html) I reported that since lysine's mg per kg estimated requirement is 17% of the total mg per kg estimated requirements for "essential" amino acids in the human body, whereas 29% of the pieces of amino acid in myoglobin are lysine, my estimate was that lysine should be emphasized when attempting to increase the body's myoglobin production potential.

The ratio of 29/17 = 1.7 for number of lysine amino acids in myoglobin as a fraction of total number of amino acids in myoglobin compared to kg per mg requirement for lysine as a fraction of total essential amino acids kg per mg requirements, is similar to the ratio I report in this post in table 1 for lysine's molecular weight as a fraction of total molecular weight in myoglobin compared to lysine molecular weight as a fraction of total molecular weight of amino acids in the human body in general.

The idea has been: improvement in terms of the amount of energy expended prior to the onset of fatigue lead to improvements in cardio health; such improvements can be facilitated by providing the body with precursors for creatine and myoglobin (which rise to high levels in the blood of marathoners during and after the marathon) prior to the body engaging in prolonged aerobic exercise.

Lysine's pre-eminent position in myoglobin, and dietary sources of lysine were discussed in the previous post; dietary sources of precursors of creatine was the subject of the post before that. In this post I discuss the importance of histidine, an important ingredient in myoglobin, and dietary sources of histidine.

The US National Rsearch Council stated in 1973, "there is no evidence that histidine is synthesized by mammals " (http://books.google.com/books?id=lIsrAAAAYAAJ&pg=PA131&lpg=PA131&dq=%22there+is+no+evidence+that+histidine%22+histidine+humans&source=bl&ots=rDVyISBP8q&sig=wB1uRjbZjbrgjf2MR-dIjFnH0mQ&hl=en&ei=JO41SpWPO6K_twe455j5Dg&sa=X&oi=book_result&ct=result&resnum=3). Wikipedia now says, "After reaching several years of age, humans begin to synthesize it (histidine) and it thus becomes a non-essential amino acid" (http://en.wikipedia.org/wiki/Histidine).

The popular and scientific literature has divided the amino acids such as those that are used to form myoglobin molecules into "essential", "conditionally essential" (or "semi-essential"), and "non-essential" groups. Histidine depending on the information source and the time at which the info source provided the info, has been classified sometimes as non-essential, sometimes as conditionally essential, and sometimes as essential.

Histidine originally was classified as non-essential, because the body is able to maintain the nitrogen balance without consuming histidine.

Then concerns began to develop, that there arise circumstances during which, due to lack of histidine in the diet and/or the body's inability to produce sufficient quantities, the body's supply of histidine becomes insufficient.

According to the 2007 WHO technical report "PROTEIN AND AMINO ACID REQUIREMENTS IN HUMAN NUTRITION" (http://whqlibdoc.who.int/trs/WHO_TRS_935_eng.pdf), "Histidine is considered to be an indispensable amino acid because of the detrimental effects on haemoglobin concentrations that have been observed when individuals are fed histidine-free diets"...Histidine was accepted in the 1985 report as an indispensable amino acid in human adults, despite controversy regarding its essentiality...Kopple & Swendseid found that nitrogen balance was negative in healthy adults and uraemic patients when diets were devoid of histidine for 25–36 days...A recent study confirmed many of these findings and showed that histidine depletion over 48 days resulted in a fall in albumin and transferrin, as well as a 24–28% decline in whole-body protein turnover. Because of the extended period of time (>56 days)".

The WHO report describes how the body deals with histidine shortages: "When a histidine-deficient diet was consumed for a prolonged period, a decrease in haemoglobin, in conjunction with a rise in serum iron,was observed...histidine pools may be maintained through the release of histidine from the degradation of haemoglobin (75), or through the reduction in haemoglobinsynthesis (82)".

Histidine is probably under-emphasized in the popular and scientific literature due to its history of being considered a "non-essential", or "conditionally essential" amino acid. Even today, the venerable Wikipedia classifies histidine as "nonessential" (http://en.wikipedia.org/wiki/Amino_acid#In_human_nutrition).
Hemoglobin and myoglobin are both involved in binding and transporting inhaled oxygen so as to make the oxygen available to muscles utilizing oxygen (aerobic means, 'requiring air'). The WHO report's finding indicates histidine shortage could result in degradation or reduction of synthesis of myoglobin, which is produced in large quantities by marathoners during the running of the marathon.

Dietary sources of histidine (http://www.nutrientfinder.com/nfsearch.php)

egg white dried flakes 1 lb 8 g

canned tuna fish 1 lb 6g

beef round 1 lb raw or braised, 5g,

pork loin chops raw 1 lb 5g,

swiss cheese 2c 5g

pork loin cooked 1 lb 4g

roasted soybean seeds, 2c 4g

pumpkin and squash seeds roasted 2c 4g

lupin seeds 2c 4gcottonseed kernels roasted 2c 3g

pheasant 1 lb 3g,

nonfat dry milk 2c 2g,

turkey roast meat raw or cooked, 1 lb, 2g

turkey pastrami 1 lb 2g

almond butter 2c 2g

dried pumpkin squash seeds 2c 2g

almond 2c 2g

roasted sunflower seeds 2c 2g

Note: dried pumpkin seeds provide half the histidine value of roasted pumpkin seeds (most 'authorities' ignore such important distinctions).

In the previous blog-post (http://davidvirgil.blogspot.com/2009/06/myoglobin-used-by-body-during-prolonged.html), I wrote that my first and second choices for providing the body with lysine, an important ingredient in the body's production of myoglobin, are soybean seeds and pistachios.

In the post before that, I listed my top choices for providing the body with the ingredients for creatine (the creatine level in marathoners rises during their run): "Pumpkin seeds (excellent source of methionine and arginine); dried egg white (excellent source of methionine and arginine); dry gelatin powder (excellent source of glycine); milk (good source of glycine); tangerine juice" (http://davidvirgil.blogspot.com/2009/06/heart-health-and-aerobic-exercise.html).

Several foods are good at providing precursors for all the biochemicals thus far of interest: creatine (glycine, arginine, and methionine), and for myoglobin (lysine, and histidine). A few foods have already been picked out as sources for creatine and lysine. What foods that have not already been picked out, should be added to the list of pre-prolonged-aerobic-exercise foods?

Yet again I make my choice with an eye towards avoiding troubles with animal foods such as cooking and cleanliness (at a later time I'll list the cooked foods that are useful for producing creatine lysine histidine etc).

Two cups of lupin seeds provide as much histidine as one pound of cooked pork loin; however, lupin seeds are difficult to find; even 'Whole Foods' does not carry lupin seeds or cottonseed kernels.

As of now, my first choice to add to my ingredient list with an eye on providing histidine in my diet, is almonds/almond-butter, which are available at Whole Foods.

My second choice would be (preferably roasted not dried) sunflower seeds.

Thus so far, my ingredients list is:

pumpkin seeds (excellent for glycine methionine & arginine for creatine; excellent for lysine and histidine for myoglobin)

Dried egg white flakes (excellent for glycine, methionine & arginine for creatine; excellent for lysine and histidine for myoglobin)

Dry gelatin powder (conventional jello mix, health-conscious whole foods jello mixes lack gelatin) (excellent source of glycine, arginine, and lysine; good source of histidine, not a good source of methionine);

Tangerine juice (facilitates absorption of methionine and glycine used to build creatine).

Milk (good source of glycine, methionine, arginine, lycine, and histidine)

Pistachios (very good source of lysine, good source of methionine, glycine, histidine, & arginine) (could not find the preferred soybean seeds at Whole Foods)

Almonds (very good source of arginine, glycine, lysine, & histidine, good source of methionine) (preferred lupin seeds unavailable at store),

Off the bat I would award points to each of these foods based on how good a source they are for the nutrients of interest and how many nutrients of interest they are a good source for; this provides me with a basis for determining how much of each substance should be used. On this basis my estimate is that the concoction should use:

1 unit milk, 1 unit tangerine juice, 1 unit pistachios, 2 units almonds, 2 units gelatin, 3 units egg white flakes, and 3 units pumpkin seeds (adjusted to provide desired consistency with flavorings added for palatibility) (unit can be tablespoon, half-cup, whatever).

The idea is to combine this (unsavory?) nutrient-rich concoction with an undisciplined consumption of whatever it is that I feel like eating.

Interesting how the stars of the show that have been discovered so far, are eggs and seeds. An egg is like a seed of a chicken.

@2009 David Virgil Hobbs