Human Protein Metabolism by Stephen Welle (auth.)

By Stephen Welle (auth.)

Human Protein Metabolism is a succinct evaluation of hundreds and hundreds of reports at the rules of protein mass and protein turnover within the human physique. The biochemistry of protein synthesis and breakdown is summarized, and the tools which are used to envision protein metabolism in people are defined, and their barriers mentioned. The ebook contains chapters that overview the consequences of food, hormones, metabolic substrates, and actual task. a number of themes of medical curiosity are lined, together with melanoma, diabetes, tissue damage, being pregnant, renal ailment, muscular dystrophies, and different stipulations. common values are awarded for turnover of proteins within the complete physique and person organs, and for turnover of many person proteins. This booklet may be a beneficial source for physiologists, nutritionists, and clinicians attracted to the law of physique protein shops in healthiness and disorder. For scientists basically drawn to the elemental facets of protein metabolism, it indicates how the fundamental wisdom is being utilized to the learn of humans.

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Another drawback ofthese methods is that no information can be gained about acute changes in protein metabolism, those occurring within a few hours after an intervention. The kinetic methods described below are necessary to overcome these limitations. Whole-Body Protein Turnover Most investigators studying protein metabolism in humans use heavy isotopes of amino acids, either radioactive or stable, as tracers. 1. Essential amino acids, those that cannot be synthesized de novo in human cells, are derived only from degradation of the body's proteins, or from dietary sources (proteins or free amino acids).

One or more amino acids from the N terminal are cleaved from most peptide chains. The N terminal often is acetylated, sometimes is acylated with formate, myristate, palmitate, or other molecules. Arginyl residues can be added at the N terminal in the absence of ribosomes. Carboxyl terminal modifications include amidation, ADP-ribosylation, acylations, prenylation, and addition of tyrosyl residues. Numerous modifications of amino acid side chains have been described. For example, certain histidine residues of actin and myosin are methylated to 3methylhistidine, and proline residues of collagen are converted to hydroxyproline.

Moreover, even within the cell it is possible that the tracer might not mix rapidly enough with amino acids from proteolysis to accurately reflect the rate of proteolysis. For example, if tracer molecules entering the cells from the extracellular compartment are more likely to flow back into the circulation than the amino acid molecules coming from protein degradation, then the enrichment in plasma would be higher than it would be ifmixing were instantaneous. In this case, protein breakdown would be underestimated.

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