Purification and characterization of the fibrinolytic principle of Agkistrodon acutus venom.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D005343:Fibrinolytic Agents / Q000302:isolation & purification; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D011506:Proteins / Q000302:isolation & purification; D012910:Snake Venoms / Q000032:analysis*
D000596:Amino Acids; D005343:Fibrinolytic Agents; D011506:Proteins; D012910:Snake Venoms