대한의생명과학회지 (Biomedical Science Letters)
- 제10권4호
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- Pages.347-351
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- 2004
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- 1738-3226(pISSN)
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- 2288-7415(eISSN)
Purification and Biochemical Characterization of a Serine Protease with Fibrinolytic Activity from Maggots of Mimela splendems
- Kwon Heun Young (Department of Clinical Laboratory Science, Catholic University of Pusan) ;
- Kim Tae Un (Department of Clinical Laboratory Science, Catholic University of Pusan)
- 발행 : 2004.12.01
초록
Maggot fibrolase (MsMg-1) was purified from the maggots of Mimela splendems using ammonium sulfate fractionation, DEAE Affi-gel affinity chromatography. This protease had a molecular weight of 85 kDa as determined by SDS-polyacrylarnide gel electrophoresis under reducing conditions. It showed strong proteolytic and fibrinolytic activities. The purified enzyme was strongly inhibited by phenylmethanesulfonyl fluoride, Mn/sup 2+/, and Zn/sup 2+/ but it was not by EDTA, EGT, Mg/sup 2+/, Ca/sup 2+/, and Li/sup 2+/ ions. In these experimental results, we have speculated that MsMg-1 is a serine protease with a strong fibrinolytic activity.