Conversion of Pig Prothrombin into Thrombin: Amino Acid Composition of the Active Enzyme

Abstract

Preparation and activation of partially purified pig prothrombin are described. The enzyme, after column chromatography in Amberlite IRC-50, showed alanine as the N-terminal residue and an [Formula: see text] of 1.50 at pH 7.0 and 280 nm.The amino acid composition of pig thrombin is reported and compared with that of bovine origin. Pig thrombin showed 1.0 mol of isoleucine to 0.6 mol of threonine as N-terminals.The effects of storage of pig prothrombin are discussed.