Abstract
A trypsin inhibitor is secreted in the pancreatic juice of the chick. Extracts from tissue have an inhibitor that corresponds to die secreted inhibitor on die basis of chromatography on DEAE-cellulose. The secretory inhibitor was purified by anion- and cation-exchange chromatography and by preparative isoelectric focusing. The purified inhibitor has 69 amino acids and is highly homologous with die secretory inhibitor from die turkey pancreas.
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