Jul 19, 1976

Purification and characterization of the fibrinolytic principle of Agkistrodon acutus venom

Biochimica Et Biophysica Acta
C Ouyang, T F Huang


By means of DEAE-Sephadex A-50 column chromatography, Agkistrodon acutus venom was separated into twelve fractions. The fibrinolytic activity was concentrated in Fraction 9. This fraction was rechromatographed on Sephadex G-75 three times 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 2.44 S was obtained by ultracentrifugation, the molecular weight of which was estimated to be 24 100, and the isoelectric point 3.8. The specific activity was four times higher than that of crude venom. The optimal pH value on fibrinolysis was 7.4. In addition to fibrinolytic activity, the purified principle also had fibrinogenolytic and caseinolytic activities. The purified fibrinolytic principle had a specific action on the a(A) chain subunit of fibrinogen, leaving the beta(B) chain and the gamma chain unaffected.

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Mentioned in this Paper

Snake Venoms
Fibrinogen Assay
Gene Products, Protein
Agkistrodon acutus
DEAE-Sephadex A-50
Electrophoresis, Disc
Assay of Fibrinolysis
Purification Aspects
Fibrinogen Complex Location

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