| Literature DB >> 15062996 |
Ricardo C H Wong1, W P Fong, T B Ng.
Abstract
Five trypsin inhibitors, with N-terminal sequences demonstrating homology to each other and exhibiting a molecular weight of 5100, 4800, 4400, 4100, and 3900, respectively, were isolated from Momordica cochinchinensis seeds with a protocol involving acid extraction, ion exchange chromatography on SP-Sepharose chromatography, and RP-HPLC on a C18 column. Specific inhibitory activity against trypsin was demonstrated by the trypsin isoinhibitors with Ki values ranging from 5.3 x 10(-8) to 1.8 x 10(-6) M. None of the isoinhibitors could be cleaved by trypsin.Entities:
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Year: 2004 PMID: 15062996 DOI: 10.1016/j.peptides.2004.01.002
Source DB: PubMed Journal: Peptides ISSN: 0196-9781 Impact factor: 3.750