Abstract
Anionic and cationic canine trypsinogens were purified from pancreatic juice by affinity chromatography with Trasylol coupled to Sepharose 4B followed by ion exchange chromatography with SP-Sephadex C-50. Automatic N-terminal amino acid sequence determination showed the following structures for the activation peptides: Thr-Pro-Thr-Asp-Asp-Asp-Asp-Lys for anionic trypsinogen, and Phe-Pro-Ile-Asp-Asp-Asp-Asp-Lys for cationic trypsinogen.

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