Abstract
A trypsin -like enzyme from the pyloric caeca of cod (Gadus morhua) was purified by affinity chromatography on CHOM Sepharose 4B. Some characteristics were established by its catalytic activity on T.A.M.E., typical enzyme substrate, and serine protease inhibitors. The enzyme had an isoelectric point of 5.30 and 5.89 and was very similar in amino acid composition to bovine trypsin, but differed in having a higher relative amount of acidic amino acids and a lower amount of basic amino acids. The enzyme also hydrolysed fish protein substrates.
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