A novel anticoagulant protein from Scapharca broughtonii.
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-100. In vitro assays with human plasma, the anticoagulant from S. broughtonii, prolonged the activated partial thromboplastin time (APTT) and inhibited the factor IX 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 26.0 kDa by gel filtration on a Sephadex G-75 column and SDSPAGE under denaturing conditions. The optimum activity in the APTT assay was exhibited at pH 7.0-7.5 and 40-45 degrees C in the presence of Ca(2+).
Jung
Won-Kyo
WK
Department of Chemistry, Pukyong National University, Busan 608-737, Korea.
Je
Jae-Young
JY
Kim
Hee-Ju
HJ
Kim
Se-Kwon
SK
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000925:Anticoagulants / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D049872:Bivalvia / Q000737:chemistry*; D001777:Blood Coagulation / Q000187:drug effects; D002118:Calcium / Q000494:pharmacology; D005164:Factor IX / Q000037:antagonists & inhibitors; D006801:Humans; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D008970:Molecular Weight; D010314:Partial Thromboplastin Time; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D013696:Temperature
D000596:Amino Acids; D000925:Anticoagulants; D011506:Proteins; D005164:Factor IX; D002118:Calcium