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- W1993586213 abstract "By means of DEAE-Sephadex column chromatography, Agkistrodon acutus venom was separated into 12 fractions. Fractions 6 and 7 had marked anticoagulant action in tests of whole blood clotting time, calcium clotting time and plasma prothrombin time. The activity of Fraction 6 was the highest. Fraction 6 was rechromatographed twice on Sephadex G-100, and a single peak was obtained. The patterns of microzone and disc electrophoresis also showed a single band. A single, symmetrical boundary with a value of 2.00 S was obtained by ultracentrifugation. The estimated molecular weight was 20 650. The isoelectric point was pH 4.7. Chemical analysis showed that the anticoagulant principle was a glycoprotein and that it was thermolabile. The anticoagulant activity of this purified principle was four times higher than that of the crude venom. This principle did not possess caseinolytic, tosyl-l-arginine methyl ester esterase, phospholipase A, phosphodiesterase, alkaline phosphomonoesterase or fibrinolytic activities." @default.
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- W1993586213 date "1972-08-01" @default.
- W1993586213 modified "2023-09-27" @default.
- W1993586213 title "Purification and properties of the anticoagulant principle of agkistrodon acutus venom" @default.
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- W1993586213 doi "https://doi.org/10.1016/0005-2795(72)90117-1" @default.
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