TY - JOUR
T1 - Simplified procedures for the isolation of HF3, bothropasin, disintegrin-like/cysteine-rich protein and a novel P-I metalloproteinase from Bothrops jararaca venom
AU - Oliveira, Ana K.
AU - Paes Leme, Adriana F.
AU - Assakura, Marina T.
AU - Menezes, Milene C.
AU - Zelanis, André
AU - Tashima, Alexandre K.
AU - Lopes-Ferreira, Mônica
AU - Lima, Carla
AU - Camargo, Antonio C.M.
AU - Fox, Jay W.
AU - Serrano, Solange M.T.
PY - 2009/6
Y1 - 2009/6
N2 - 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.
AB - 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.
KW - Fibrinogenolysis
KW - Hemorrhage
KW - Proteolysis
KW - Snake venom metalloproteinase
UR - https://www.scopus.com/pages/publications/67349143081
U2 - 10.1016/j.toxicon.2009.02.019
DO - 10.1016/j.toxicon.2009.02.019
M3 - Article
C2 - 19254739
AN - SCOPUS:67349143081
SN - 0041-0101
VL - 53
SP - 797
EP - 801
JO - Toxicon
JF - Toxicon
IS - 7-8
ER -