@article{ref1,
title="Purification and partial characterization of a thrombin-like/gyroxin enzyme from bushmaster (Lachesis muta rhombeata) venom",
journal="Toxicon: Journal of the International Society on Toxinology",
year="1996",
author="Aguiar, A. S. and Alves, C. R. and Melgarejo, A. and Giovanni-de-Simone, S.",
volume="34",
number="5",
pages="555-565",
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).<p /><p>Language: en</p>",
language="en",
issn="0041-0101",
doi="10.1016/0041-0101(95)00159-X",
url="http://dx.doi.org/10.1016/0041-0101(95)00159-X"
}