title: [Trypsin-, chymotrypsin-like proteinases in fishes].
abstract: Recent data on the nature of trypsin-, chymotrypsin-like proteinases of fish are generalized. Localization and secretion of these enzymes in pyloric appendages of fish are considered in detail. Trypsin and chymotrypsin are in the state of proenzymes and transform into the active form by means of their own proteolytic factors. It is observed that the classical methods for isolation of individual chymotrypsin and trypsin cannot be used in the case of fish, since the fish enzymes are stable in the neutral and low-alkaline media and unstable in the acid medium. This is, first of all, accounted for by differences in the physicochemical characteristics of the test enzymes. New data on the biospecific chromatography of serine proteinases of lower invertebrates are presented. Biospecific sorbents used for isolating enzymes from mammals are not always convenient for purification of fish serine proteinases. This evidences for considerable differences in their active sites and, probably, in their binding sites, whose nature is responsible for the specificity and is important for the selective chromatography of enzymes.
authors.forename: M V
authors.initials: MV
authors.lastname: Kolodzeĭskaia
authors.forename: T N
authors.initials: TN
authors.lastname: Pivnenko
mesh_terms: D000818:Animals; D002918:Chymotrypsin / Q000302:isolation & purification / Q000378:metabolism*; D005399:Fishes / Q000378:metabolism*; D007700:Kinetics; D013045:Species Specificity; D014357:Trypsin / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D002918:Chymotrypsin; D014357:Trypsin
vernacular_title: Tripsin-, khimotripsinpodobnye proteinazy ryb.