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A novel extracellular protease with fibrinolytic activity from the culture supernatant of Cordyceps sinensis : purification and characterization
Author(s) -
Li Huaping,
Hu Zheng,
Yuan Jianglan,
Fan Handong,
Chen Wei,
Wang Shijia,
Zheng Shanshan,
Zheng Zhongliang,
Zou Guolin
Publication year - 2007
Publication title -
phytotherapy research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 129
eISSN - 1099-1573
pISSN - 0951-418X
DOI - 10.1002/ptr.2246
Subject(s) - biochemistry , protease , serine protease , casein , plasmin , enzyme , cordyceps , plasminogen activator , cysteine , chemistry , biology , endocrinology , food science
A novel serine protease with fibrinolytic activity named CSP was purified from the culture supernatant of the fungus Cordyceps sinensis , a kind of Chinese herbal medicine. Analysis of the purified enzyme by SDS‐PAGE indicated that CSP was a single polypeptide chain with an apparent molecular weight of 31 kDa, and N ‐terminal sequencing revealed that the first ten amino acid residues of the enzyme were Ala‐Leu‐Ala‐Thr‐Gln‐His‐Gly‐Ala‐Pro‐Trp‐. When casein was used as a substrate, the proteolytic activity of CSP reached its maximum at pH 7.0 and 40 °C. The effect of chemical agents on the enzyme activity indicated that CSP is a serine protease with a free cysteine residue near the active site. It hydrolysed fibrinogen, fibrin and casein with a high efficiency, while hydrolysing bovine serum albumin (BSA) and human serum albumin (HSA) to a lesser extent. CSP was found to be a plasmin‐like protease, but not a plasminogen activator, and it preferentially cleaved the A α chain of fibrinogen and the α ‐chain of fibrin. Therefore, the extracellular protein CSP may represent a potential new therapeutic agent for the treatment of thrombosis. Copyright © 2007 John Wiley & Sons, Ltd.