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A new peptidic protease inhibitor from Vicia faba seeds exhibits antifungal, HIV‐1 reverse transcriptase inhibiting and mitogenic activities
Author(s) -
Ye X. Y.,
Ng T. B.
Publication year - 2002
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.425
Subject(s) - chymotrypsin , trypsin , protease , protease inhibitor (pharmacology) , vicia faba , reverse transcriptase , trypsin inhibitor , biochemistry , enzyme inhibitor , biology , enzyme , microbiology and biotechnology , peptide , kunitz sti protease inhibitor , molecular mass , chemistry , virology , human immunodeficiency virus (hiv) , rna , botany , antiretroviral therapy , viral load , gene
A new trypsin–chymotrypsin inhibitor, with an N ‐terminal sequence showing some differences from the previously reported trypsin–chymotrypsin inhibitor, was isolated from the broad bean Vicia faba . The inhibitor was a peptide with a molecular mass of 13 kDa. It was adsorbed on Affi‐gel blue gel and CM‐Sepharose. It exerted antifungal activity toward Mycosphaerella arachidicola and Physalospora piricola . In addition, the trypsin–chymotrypsin inhibitor elicited a mitogenic response from mouse splenocytes and inhibited the activity of human immunodeficiency virus‐1 reverse transcriptase. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.