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.
Tanizaki
M M
MM
Serviço de Bioquimica, Instituto Butantan, São Paulo, Brasil.
Kawasaki
H
H
Suzuki
K
K
Mandelbaum
F R
FR
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