Localization and biochemical characterization of pharyngeal protease in the polychaetous annelid Glycera convoluta

In Glycera convoluta Keferstein, pharyngeal protease is secreted by the glandular epithelial cells, as clearly demonstrated by microscopic observation of the digestion of a prestained gelatin film by fresh tissue sections of the organ. The enzyme, extracted by affinity chromatography on Sepharose-?-aminocaproïc-D-tryptophan, acts on substrates hydrolyzable by α-chymotrypsin such as N-benzoyl-L-tyrosine ethyl ester and carboxyl-propionyl-phenylalanine-p-nitroanilide, and can be considered as a chymotrypsin-like enzyme.