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Title: [Isolation and properties of trypsin isoinhibitors from kidney beans]. Author: Mosolov VV, Fedurkina NV, Valueva TA. Journal: Biokhimiia; 1977 Jul; 42(7):1201-11. PubMed ID: 907794. Abstract: Two isoinhibitors (II and III-B) have been isolated from kidney bean (Phaseolus vulgaris L.) in a highly purified state. Both were active against trypsin and chymotrypsin to the same extent. Their amino acid composition is characterized by a high content of half-cystine, aspartic acid (or asparagine) and serine, by the absence of valine, methionine and tryptophan. Glycine and serine were N-terminal in II and III-B respectively. Both isoinhibitors have C-terminal leucine.[Abstract] [Full Text] [Related] [New Search]