title: Biophysical properties and amino acid composition of Bothrops protease A, a proteolytic enzyme isolated from the venom of the snake Bothrops jararaca (jararaca).
abstract: Bothrops protease A, an arginine-ester hydrolase, is active on protamine, gelatin and insulin and was isolated from the venom of Bothrops jararaca in a homogeneous state, as judged by polyacrylamide gel electrophoresis and ultracentrifugal analyses. The enzyme has a molecular weight of 65,000 and a pI of 3.55. The enzyme is a glycoprotein whose amino acid content corresponds to 55% of the molecular weight.
mesh_terms: D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D003435:Crotalid Venoms / Q000032:analysis*; D010450:Endopeptidases / Q000032:analysis*; D008970:Molecular Weight; D012697:Serine Endopeptidases
chemical_list: D000596:Amino Acids; D003435:Crotalid Venoms; D010450:Endopeptidases; C038929:Bothrops jararaca protease A; D012697:Serine Endopeptidases