Abstract
Proteins within animal and bacterial cells vary widely in their rates of degradation, and these differences appear to reflect differences in protein conformations. For example, half-lives of intracellular proteins as well as serum appear to correlated with their inherent sensitivity to various proteolytic enzymes. We have also found that the half-lives of proteins are related to their net charge. In various tissues and in rat serum, proteins with acidic isoelectric points are degraded more rapidly that neutral or basic ones. Isoelectric point and subunit molecular weight are two independent parameters that influence degradative rates of proteins.
Published Version
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