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| Peptide Forum Peptide Forum. Ask and discuss questions on peptide protocols, custom peptide synthesis, peptide identification and peptide sequencing. |
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#1
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| I need to know this for a bio test and am not sure which it is. Thanks! |
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#2
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| Pepsin is an enzyme whose zymogen (pepsinogen) is released by the chief cells in the stomach and that degrades food proteins into peptides. |
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#3
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| Pepsin is relatively non-specific although it does have a preference for cleaving after hydrophobic amino acids in protein,peptide, polypeptide . Pepsin breack peptide bond between hydrophobic peptide like phenylalanine, tryptophan, Tyrosine. Pepsin will also preferentially cleave at the carboxyl side of phenylalanine and leucine and to a lesser extent at the carboxyl side of glutamic acid residues.Amidation of the C-terminal carboxyl group prevents hydrolysis by pepsin. or e.g. :- Pepsin Cleaves Phe1-Val, Gln4-His, Glu13-Ala, Ala14-Leu, Leu15-Tyr, Tyr16-Leu, Gly23-Phe, Phe24-Phe and Phe25-Tyr bonds in the B chain of insulin. Regards
__________________ Kunal Pandya |
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| break , pepsin , peptides , polypeptides , protein |
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