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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Bothrops jararaca antithrombin: Isolation, characterization and comparison with other animal antithrombins

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Author(s):
de Morais, Karen Batista [1, 2] ; Vieira, Carolina Okamoto [1, 2] ; Hirata, Isaura Yoshico [3] ; Tanaka-Azevedo, Anita Mitico [2]
Total Authors: 4
Affiliation:
[1] Univ Sao Paulo, Dept Fisiol, Inst Biociencias, BR-05508900 Sao Paulo - Brazil
[2] Inst Butantan, Lab Fisiopatol, BR-05503900 Sao Paulo - Brazil
[3] Univ Fed Sao Paulo, Dept Bioquim, BR-04044020 Sao Paulo - Brazil
Total Affiliations: 3
Document type: Journal article
Source: COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY; v. 152, n. 2, p. 171-176, FEB 2009.
Web of Science Citations: 3
Abstract

Antithrombin was purified from Bothrops jararaca plasma by affinity chromatography using HiTrap Heparin HP column, and its molecular weight, amino-terminal sequence, carbohydrate content, isoelectric point, inhibition of bovine thrombin, and immunological properties were studied and compared with previously described antithrombins. B. jararaca antithrombin is a single-chain glycoprotein with a total carbohydrate content of 18%. The molecular weight from SDS-PAGE was 61 kDa and the inhibitor exhibited an acidic isoelectric point (4.5). The amino-terminal sequence has been determined as His-Glu-Ser-Ser-Val-Gln-Asp-Ile-Ile-Thr, which is highly homologous to the terminal sequences of other animal antithrombins, indicating high amino acid conservation among several animals. Immunological cross-reactivity was observed among fish, frog, chicken, human, non-venomous snake and B. jararaca antithrombins. B. jararaca antithrombin showed inhibitory activity upon human and B. jararaca coagulation and amidolytic substrate S-2238. (c) 2008 Elsevier Inc. All rights reserved. (AU)