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Role of RNA in Protein Synthesis
Markedly increased synthesis of α2 and β globulins and α1, α2, and β glycoglobulins occurs during pneumococcal sepsis in the rat simultaneously with decreased albumin formation, diminished tritiated leucine incorporation into muscle protein, and enhanced excretion of nitrogen. This augmented synthesis of specific serum proteins does not become evident until fever and bacteremia develop, and it appears to be a fundamental aspect of host response to a proliferating bacterial infection in that it occurs even in rats fed a protein-deficient (6% protein) diet after weaning and before exposure to Diplococcus pneumoniae.
The majority of protein is digested, and the amino acids not used for gut fuel are metabolized in the intestinal mucosal cells and transported by the portal vein to the liver for protein synthesis or gluconeogenesis.12 In the liver, nonessential amino acids are largely deaminated, and the amino group (nitrogen) removed is converted into urea for excretion in the urine.13 It has been shown that in subjects without and with mild type 2 diabetes, ~5070% of a 50-g protein meal is accounted for over an 8-hour period by deamination in the liver and intestine and synthesis to urea.14 It has been assumed that the remaining carbon skeletons from the nonessential amino acids are available for glucose synthesis, which would then enter into the general circulation.
quiz protein synthesis - Biology Junction
Humans can degrade all the amino acids that are commonly found in proteins, but we have very limited synthetic capacity. However, it may be possible to use surplus nitrogen from other sources to make good a dietary deficiency in some of these "non-essential" amino acids, providing that the total nitrogen intake is sufficient. In addition, a few amino acids are degraded to form other amino acids (for example, phenylalanine is metabolised initially to tyrosine) so that tyrosine is essential on a minimal diet, but becomes non-essential if sufficient phenylalanine is eaten. Tyrosine is therefore described as a "conditionally essential" amino acid.
There are four different nitrogen bases, adenine, thymine, cytosine and guanine. The synthesis of a particular protein such as insulin is determined by the sequence in which these bases are repeated (see fig.
How Much Protein is TOO Much? All About Nitrogen Balance
The recommended minimal protein intake required to achieve nitrogen balance in healthy adults is about 50g per day, although in developed countries many people may eat double this amount. This compares with an average daily protein turnover of about 250g per day. Human proteins have very different lifetimes. Total body protein is about 11kg, but about 25% of this is collagen, which is metabolically inert. A typical muscle protein might survive for three weeks, but many liver enzymes turn over in a couple of days. Some regulatory enzymes have half-lives measured in hours or minutes. The majority of the amino acids released during protein degradation are promptly re-incorporated into fresh proteins. Net protein synthesis accounts for less than one third of the dietary amino acid intake, even in rapidly growing children consuming a minimal diet. Most of the ingested protein is ultimately oxidised to provide energy, and the surplus nitrogen is excreted, a little as ammonia but mostly as urea.
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