Purification of a proteinase inhibitor from the plasma of Bothrops jararaca (jararaca).
A proteinase inhibitor was isolated from the plasma of Bothrops jararaca by three chromatographic steps: DEAE Sephacel, Phenyl Sepharose and Bio Gel P200. It inhibited caseinolytic and hemorrhagic activity of the whole venom of B. jararaca. Proteolytic activity of bothropasin and J protease, both metalloproteinases of the venom, were neutralized by the inhibitor. The J protease-inhibitor complex was isolated by gel filtration chromatography in HPLC and the electrophoresis pattern of this complex showed that the interaction between enzyme and inhibitor is not covalent.
Serviço de Bioquimica, Instituto Butantan, São Paulo, Brasil.
M M
MM
Tanizaki
H
H
Kawasaki
K
K
Suzuki
F R
FR
Mandelbaum
D000645:Ammonium Sulfate; D000818:Animals; D002364:Caseins / Q000737:chemistry; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003435:Crotalid Venoms / Q000737:chemistry / Q000633:toxicity; D010450:Endopeptidases / Q000302:isolation & purification; D006470:Hemorrhage / Q000139:chemically induced; D006868:Hydrolysis; D051379:Mice; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000097:blood / Q000302:isolation & purification*; D012911:Snakes / Q000097:blood*
D002364:Caseins; D003435:Crotalid Venoms; D011480:Protease Inhibitors; D010450:Endopeptidases; D000645:Ammonium Sulfate