Purification and Specificity of Porcine Enterokinase

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Purification and specificity of porcine enterokinase.

Enterokinase (enteropeptidase, EC 3.4.4.8) has been purified from porcine duodenal extracts by chromatography on DEAE-cellulose, carboxymethyl cellulose, Sephadex G-100, and Sephadex G-200. The final product was found to be homogeneous by a number of tests. Its specific activity against trypsinogen (nanomoles of trypsinogen activated per 30 min per mg) was 6550, which represented a 650-fold pur...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1971

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)61965-9