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Simplified procedures for the isolation of HF3, bothropasin, disintegrin-like/cysteine-rich protein and a novel P-I metalloproteinase from Bothrops jararaca venom

2009; Elsevier BV; Volume: 53; Issue: 7-8 Linguagem: Inglês

10.1016/j.toxicon.2009.02.019

1879-3150

Ana K. Oliveira, Adriana Franco Paes Leme, Marina T. Assakura, Milene C. Menezes, André Zelanis, Alexandre K. Tashima, Mônica Lopes‐Ferreira, Carla Lima, Antônio Carlos Martins de Camargo, Jay W. Fox, Solange M.T. Serrano,

Biochemical and Structural Characterization

HF3 and bothropasin are P-III hemorrhagic snake venom metalloproteinases (SVMPs) of Bothrops jararaca. The DC protein is composed of the disintegrin-like/cysteine-rich domains derived from the autolysis of P-III SVMPs. Here we describe simplified procedures for the isolation of HF3, bothropasin, the DC protein, and BJ-PI, a novel P-I SVMP. The isolated proteins were identified by mass spectrometry. BJ-PI is a potent caseinolytic enzyme devoid of hemorrhagic activity. HF3, bothropasin and BJ-PI show distinct fibrinogenolytic activities.