Arginine methionine

It is a single chain peptide hormone, isolated in pure form and contains tyrosine, tryptophan, cystine, arginine, methionine of approximately 25,000 molecular weight. It has a direct effect upon the breasts immediately after the delivery of baby and in conjunction with other hormones, it stimulates the breast to secrete milk. 

The interassay variation was assessed in a plasma pool, which was stored at -20°C and analyzed 26 times over an 8-month period. The coefficients of variation (CVs) ranged from 6.1 to 8.9% with the following exceptions glutamine decreases steadily from 587 to 447 pmol/1 with a concomitant increase of glutamic acid from 62 to 164 pmol/1. Cystine decreased from 35 pmol/1 to undetectable. Tryptophan, arginine, methionine, asparagine, and proline had CVs slightly in excess of 10%. 

There are 22 different AAs in the body of the bird, 10 of which are essential AA (EAA arginine, methionine, histidine, phenylalanine, isoleucine, leucine, lysine, threonine, tryptophan and valine), i.e. cannot be manufactured by the body and must be derived from the diet. Cystine and tyrosine are semi-essential in that they can be synthesized from methionine and phenyla-... 

The failure of amino acid degradation to go to completion and the relation between maximal destruction and temperature might be attributed to the fact that individual amino acids reacted at different rates at different temperatures. For example certain amino acids, leucine, arginine, methionine, and lysine showed little or no detectable reaction at 100°C after one hour, while others were reactive at this temperature(Table X). At higher temperatures, rate of amino acid degradation was measurable and proportional to the temperature of the reaction. 

Such chemical changes may lead to compounds that are not hydrolyzable by intestinal enzymes or to modifications of the peptide side chains that render certain amino acids unavailable. Mild heat treatments in the presence of water can significantly improve the protein s nutritional value in some cases. Sulfur-containing amino acids may become more available and certain antinutritional factors such as the trypsin inhibitors of soybeans may be deactivated. Excessive heat in the absence of water can be detrimental to protein quality for example, in fish proteins, tryptophan, arginine, methionine, and lysine may be damaged. A number of chemical reactions may take place during heat treatment including decomposition, dehydration of serine and threonine, loss of sulfur from cysteine, oxidation of cysteine and methio-... 

Essential Arginine Methionine Phenylalanine" Histidine Isoleucine Leucine Lysine... 

Glucogenic amino acids Glycine, serine, cysteine, alanine, aspartate, histidine, glutamate, proline, arginine, methionine, threonine and valine are glucogenic. 

Blood meal is a chocolate-coloured powder with a characteristic smell. It contains about 800 g/kg of protein, small amounts of ash and oil, and about 100 g/kg of water. It is important nutritionally only as a source of protein. Blood meal is one of the richest sources of lysine and a rich source of arginine, methionine, cystine and leucine, but it is deficient in isoleucine and contains less glycine than fish, meat, or meat and bone meals. Owing to the poor balance of amino acids, its biological value is low in addition, it has a low digestibility. It has the advantage, in certain situations, that its protein has a very low rumen degradability (about 0.20). 

From simple animals like protozoans, through more complex ones such as worms and insects, to the most highly evolved vertebrates, there appear to be 9 or 10 essential amino acids that must be supplied from an outside (exogenous) source (Prosser, 1973a). These essential amino acids are valine, leucine, isoleucine, lysine, arginine, methionine, threonine, phenylalanine, tryptophan, and histi-... 

Modification of tyrosine, threonine/serine, arginine, methionine residues etc... 

Most of the bacteria, yeasts, molds, and higher fungi of interest for SCP production are deficient in methionine and must be supplemented with this amino acid to be suitable for animal feeding or human food appHcations. Also, lysine—arginine ratios should be adjusted in poultry rations in which yeast SCP is used (62). Human feeding studies have shown that only limited quantities of yeast such as Candida utilis can be added to food products without adverse effects on flavor (63). 

Histone methylation is a common posttranslational modification fond in histones. Histone methylations have been identified on lysine and arginine residues. In case of lysines S-adenosyl-methionine (SAM) dependent methyl transferases catalyze the transfer of one, two or three methyl groups. Lysine methylation is reversible and lysine specific demethylases have been... 

Creatinine is formed in muscle from creatine phosphate by irreversible, nonenzymatic dehydration and loss of phosphate (Figure 31-6). The 24-hour urinary excretion of creatinine is proportionate to muscle mass. Glycine, arginine, and methionine all participate in creatine biosynthesis. Synthesis of creatine is completed by methylation of guanidoacetate by S-adenosylmethio-nine (Figure 31-6). 

The biosynthesis of two major classes of red tide toxins, saxitoxin analogs and brevetoxins, have been studied. It was shown that saxitoxin is biosynthesized from arginine, acetate, and methionine methyl group. Brevetoxins were shown to be unique polyketides, which are probably biosynthesized from dicarboxylic acids. Some details of the biosynthetic mechanism have been elucidated. 

Aminopeptidase A is another brush border membrane enzyme which has been the subject of various studies [79,81,83-86], It has been found in the intestinal brush border membrane of humans, rabbits, rats, and pigs and is active against peptides with acidic amino acids at the amino terminus. Its activity against dipeptides is more limited. Shoaf et al., isolated three rat brush border aminopeptidases with distinct but somewhat overlapping substrate specificities. These enzymes had preference for dipeptides containing methionine, arginine, or aspartic acid and glycine. The optimal pH for activity of aminopeptidase was reported to be 7-8. 

Included amino acids were alanine, arginine, aspartic acid, asparagine, glutamine, glutamic acid, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, proline, serine, threanine, tryptophan, tyrosine, and valine. 

The information contained in the DNA (i.e., the order of the nucleotides) is first transcribed into RNA. The messenger RNA thus formed interacts with the amino-acid-charged tRNA molecules at specific cell organelles, the ribosomes. The loading of the tRNA with the necessary amino acids is carried out with the help of aminoacyl-tRNA synthetases (see Sect. 5.3.2). Each separate amino acid has its own tRNA species, i.e., there must be at least 20 different tRNA molecules in the cells. The tRNAs contain a nucleotide triplet (the anticodon), which interacts with the codon of the mRNA in a Watson-Crick manner. It is clear from the genetic code that the different amino acids have different numbers of codons thus, serine, leucine and arginine each have 6 codewords, while methionine and tryptophan are defined by only one single nucleotide triplet. 

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