Abstract：
:A novel protease inhibitor, designated mungoin, with both antifungal and antibacterial activities, and exhibiting a molecular mass of 10kDa in SDS-polyacrylamide gel electrophoresis, was isolated from mung bean (Phaseolus mungo) seeds. The isolation procedure involved a combination of extraction, ammonium sulfate precipitation, ion exchange chromatography on CM-Sephadex, and high-performance liquid chromatography (HPLC) on SP-Toyopearl. Its isoelectric point was estimated to be 9.8 by isoelectric focusing. Its N-terminal amino acid sequence was determined to be EMPGKPACLDTDDFCYKP, demonstrating some resemblance to the C-terminal sequences of other protease inhibitors and inhibitor precursors from leguminous plants. It exerted a potent inhibitory action toward a variety of fungal species including Physalospora piricola, Mycosphaerella arachidicola, Botrytis cinerea, Pythium aphanidermatum, Sclerotium rolfsii and Fusarium oxysporum, as well as an antibacterial action against Staphylococcus aureus. In addition, this novel plant protease inhibitor displayed anti-proliferative activity toward tumor cells.
journal_name
Peptidesjournal_title
Peptidesauthors
Wang S,Lin J,Ye M,Ng TB,Rao P,Ye Xdoi
10.1016/j.peptides.2006.07.013subject
Has Abstractpub_date
2006-12-01 00:00:00pages
3129-36issue
12eissn
0196-9781issn
1873-5169pii
S0196-9781(06)00343-3journal_volume
27pub_type
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