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

Autor(es)

de Morais, Karen Batista ^{[1, 2]} ; Vieira, Carolina Okamoto ^{[1, 2]} ; Hirata, Isaura Yoshico ^[3] ; Tanaka-Azevedo, Anita Mitico ^[2]

Afiliação do(s) autor(es)

^[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

• Tipo de documento: Artigo Científico
• Fonte: COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY; v. 152, n. 2, p. 171-176, FEB 2009.
• Citações Web of Science: 3

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. (AU)

• Processo FAPESP: 04/02224-4 - Estudo de estrutura e função de proteínas envolvidas no mecanismo de coagulação da serpente Bothrops jararaca
• Beneficiário: Anita Mitico Tanaka-Azevedo
• Modalidade de apoio: Auxílio à Pesquisa - Regular