Conversion of Pig Prothrombin into Thrombin: Amino Acid Composition of the Active Enzyme
- 1 April 1974
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 52 (4) , 336-344
- https://doi.org/10.1139/o74-051
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 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.Keywords
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