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Functional and Structural Characterization of a Prokaryotic Peptide
Functional and Structural Characterization of a Prokaryotic Peptide

... inhibitors, and peptidase inhibitors and thereby determine their bioavailability and pharmacokinetics. Certain drugs with an intrinsic low oral bioavailability like L-DOPA and acyclovir have by coupling to an amino acid (L-DOPA-Phe and Val-acyclovir) turned into substrates of peptide transporters wi ...
Relationship between relative protein value and some in vitro in
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... Ramachandra et al., 1977; Marable and Sanzone, 1981). It has been demonstrated that mammalian intestine can take up small peptides in addition to free AAs. Several kinetic advantages associated with the small peptide absorption as against the free AA absorption (Adibi, 1971; Matthews et al., 1969), ...


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Slide
Slide

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Proteolysis



Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Low pH or high temperatures can also cause proteolysis non-enzymatically.Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes, as well as preventing the accumulation of unwanted or abnormal proteins in cells. Consequently, dis-regulation of proteolysis can cause diseases, and is used in some venoms to damage their prey.Proteolysis is important as an analytical tool for studying proteins in the laboratory, as well as industrially, for example in food processing and stain removal.
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