Biophysical properties and amino acid composition of Bothrops protease A, a proteolytic enzyme isolated from the venom of the snake Bothrops jararaca (jararaca)

Abstract

A. P. Reichl, M. T. Assakura and F. R. Mandelbaum. Biophysical properties and amino acid composition of Bothrops protease A, a proteolytic enzyme isolated from the venom of the snake Bothrops jararaca (jararaca). Toxicon 21, 421–427, 1983. — Bothrops protease A, an arginine-ester hydrolase, is active on protamine, gelatine 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.