Isolation of Human Trypsin by Affinity Chromatography

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Abstract
A method is described to prepare an affinity adsorbent for human trypsin by coupling bovine pancreatic trypsin inhibitor (Kunitz) to CNBr-activated Sepharose. The highly selective adsorbent permitted the rapid isolation of trypsin from an activated extract of human pancreas. The trypsin obtained was completely free of chymotryptic activity and of sufficient purity to serve as a standard for the development of a specific radioimmunoassay for human trypsin.

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