Biomedical Science Letters (대한의생명과학회지)

The Korean Society for Biomedical Laboratory Sciences (대한의생명과학회)
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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)
  • Published : 2004.12.01
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Abstract

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.

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