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

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

Author Morais, Karen Batista de Google Scholar
Vieira, Carolina Okamoto Google Scholar
Hirata, Izaura Yoshico Autor UNIFESP Google Scholar
Tanaka-Azevedo, Anita Mitico Google Scholar
Institution Inst Butantan
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
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.
Keywords Antithrombin
Amino acid sequence
Snake plasma
Bothrops jararaca
Language English
Sponsor Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
Grant number FAPESP: 04/02224-4
Date 2009-02-01
Published in Comparative Biochemistry and Physiology B-biochemistry & Molecular Biology. New York: Elsevier B.V., v. 152, n. 2, p. 171-176, 2009.
ISSN 1096-4959 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 171-176
Access rights Closed access
Type Article
Web of Science ID WOS:000263140700009

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