Please use this identifier to cite or link to this item:
Type: Artigo de periódico
Title: Purification And Partial Characterization Of A Thrombin-like Enzyme, Balterobin, From The Venom Of Bothrops Alternatus.
Author: Smolka, M B
Marangoni, S
Oliveira, B
Novello, J C
Abstract: A thrombin-like enzyme, balterobin, was purified from the venom of Bothrops alternatus. The purification steps included Sephadex G-75, heparin-sepharose and reverse phase HPLC C-18 column. Balterobin showed an apparent molecular weight of 30,000 in non-reduced conditions and displays a specific coagulant activity of 32.8 NIH units/mg over bovine fibrinogen. It also exhibits arginine amidase activity on DL-BAPNA. Like thrombin-like enzymes from other snakes, balterobin possesses valine as N-terminal residue, and is inhibited by PMSF.
Subject: Animals
Crotalid Venoms
Molecular Weight
Rights: fechado
Identifier DOI: 
Date Issue: 1998
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

Files in This Item:
File SizeFormat 
pmed_9690798.pdf207.21 kBAdobe PDFView/Open

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.