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 serineprotease inhibitors. The enzyme had an isoelectricpoint 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. Hie enzyme also hydrolysedfish protein substrates.
CITATION STYLE
Beiräo, L. H., Mackie, L. M., Teixeira, E., & Damian, C. (2001). Purification and Characterisation of Trypsin-Like Enzyme from the Pyloric Caeca of Cod (Gadus morhua) II. Brazilian Archives of Biology and Technology, 44(1), 33–40. https://doi.org/10.1590/S1516-89132001000100005
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