Citation

Aguiar AS, Alves CR, Melgarejo A, Giovanni-de-Simone S. Toxicon 1996; 34(5): 555-565.

Affiliation

Instituto Vital Brazil, Niterói RJ, Brazil.

Copyright

(Copyright © 1996, Elsevier Publishing)

DOI

10.1016/0041-0101(95)00159-X

PMID

8783450

Abstract

The acidic coagulating enzyme of the L. m. rhombeata venom was purified to homogeneity using one step on preparative isoelectric focusing followed by gel permeation on a high performance liquid chromatography system. The enzyme focused with pIs 3.1-5.0 and had a molecular mass of 47,000 mol. wt as determined by high performance liquid gel-filtration chromatography and about 45,000 mol. wt as judged by sodium dodecyl sulfate-polyacrylamide-gel electrophoresis. The enzyme is a glycoprotein containing sialic acid and 12.4% of neutral carbohydrates. The 30 N-terminal amino acid sequence of the L. m. rhombeata protein shows 100% identity with L. m. muta gyroxin and considerable sequence homology with gyroxin and thrombin-related proteins. The enzyme exhibits strong N-p-tosyl-L-arginine methyl esterase activity, hydrolyses tripeptide nitroanilide derivatives weakly or not at all, and cleaves specifically the fibropeptide A (alpha-chain).

Language: en