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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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A Novel Anticoagulant Protein from Scapharca broughtonii

  • Jung, Won-Kyo (Department of Chemistry, Pukyong National University) ;
  • Je, Jae-Young (Department of Chemistry, Pukyong National University) ;
  • Kim, Hee-Ju (Department of Chemistry, Pukyong National University) ;
  • Kim, Se-Kwon (Department of Chemistry, Pukyong National University)
  • Published : 2002.03.31
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Abstract

An anticoagulant protein was purified from the edible portion of a blood ark shell, Scapharca broughtonii, by ammonium sulfate precipitation and column chromatography on DEAE-Sephadex A-50, Sephadex G-75, DEAE-Sephacel, and Biogel P-l00. In vitro assays with human plasma, the anticoagulant from 'S. broughtonii, prolonged the activated partial thromboplastin time (APTT) and inhibited the factor LX in the intrinsic pathway of the blood coagulation cascade. But, the fibrin plate assay did not show that the anticoagulant is a fibrinolytic protease. The molecular mass of the purified S. broughtonii anticoagulant was measured to be about 26.0kDa by gel filtration on a Sephadex G-75 column and SDS-PAGE under denaturing conditions. The optimum activity in the APTT assay was exhibited at pH 7.0-7.5 and $40-45^{\circ}C$ in the presence of $Ca^{2+}$.

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References

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