Bothrops jararaca antithrombin: Isolation, characterization and comparison with other animal antithrombins
Data
2009-02-01
Autores
Hirata, Izaura Yoshico 
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Artigo
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Resumo
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.
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Comparative Biochemistry and Physiology B-biochemistry & Molecular Biology. New York: Elsevier B.V., v. 152, n. 2, p. 171-176, 2009.