Venom from southern copperhead snake (Agkistrodon contortrix contortrix). I. Characterization of a protease that preferentially releases fibrinopeptide B.
Using gel permeation chromatography with high performance liquid chromatograph (HPLC), a highly purified preparation of a protease has been obtained from the venom of the southern copperhead snake (Agkistrodon contortrix contortrix). Both gel permeation chromatography with HPLC and sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that it had an apparent Mr of 60,000-64,000. It consisted of a single polypeptide chain. The activity was inhibited by dithiothreitol. It neither induced platelet aggregation nor activated plasma factor XIII. It cleaved fibrinopeptide B at a rate much faster than fibrinopeptide A from fibrinogen. This specificity was steadily lowered when the incubation temperature was elevated from 0 degrees C to 45 degrees C. Fibrinopeptides were released only at neutral pH.
Shimizu
A
A
Laboratory of Biological Chemistry, Tokyo Institute of Technology, Japan.
Jimenez
E C
EC
Takagi
J
J
Inada
Y
Y
Saito
Y
Y
D000818:Animals; D002417:Cattle; D003435:Crotalid Venoms / Q000302:isolation & purification* / Q000494:pharmacology; D005176:Factor XIII / Q000378:metabolism; D005340:Fibrinogen / Q000378:metabolism*; D005345:Fibrinopeptide B / Q000378:metabolism*; D066298:In Vitro Techniques; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000494:pharmacology; D010974:Platelet Aggregation / Q000187:drug effects
D003435:Crotalid Venoms; D005345:Fibrinopeptide B; D005340:Fibrinogen; D005176:Factor XIII; D010447:Peptide Hydrolases