The activation of chymotrypsinogen by papain

descriptionPublicationkeyboard_double_arrow_right Article 01 Nov 1970 English Publisher:Canadian Science PublishingJournal:Canadian Journal of Biochemistry, volume 48, pages 1,208-1,213 (issn: 0008-4018,

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Authors: M C, Shaw; T, Kay; T, Viswanatha;

doi: 10.1139/o70-188

pmid: 5475874

The activation of chymotrypsinogen by papain

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Abstract

Papain has been found to activate bovine chymotrypsinogen A. The optimal conditions for the activation are pH 5.0, temperature 23 °C, and enzyme/substrate ratio 1:20. The chymotrypsin obtained by the papain activation has been isolated. A significant difference between this enzyme and α-chymotrypsin is the absence of the three amino acids (Ser, Gly, and Leu) occupying the C-terminal of the A-chain of the former.

Keywords

Chromatography, Enzyme Precursors, Chemical Phenomena, Temperature, Phosphorus Isotopes, Hydrogen-Ion Concentration, Methylcellulose, Chemistry, Papain, Chymotrypsin, Amino Acids

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