title: Characteristics of a proteinase from ovarian fluid of the lumpsucker (Cyclopterus lumpus L.).
abstract: 1. A proteinase has been isolated from the ovarian fluid of the lumpsucker (Cyclopterus lumpus). 2. The enzyme was purified essentially to homogeneity by a one step purification procedure using anion-exchange chromatography. 3. The mol. wt of the denatured enzyme is approximately 20,000 as judged by SDS-polyacrylamide gel electrophoresis. 4. The enzyme is inhibited by serine-proteinase inhibitors and acts in the manner of a trypsin-type proteinase both with respect to specific peptide substrates and enzyme inhibitors. 5. The lumpsucker proteinase exhibits low general proteolytic activity but acts effectively on the specific chromogenic peptide substrates.
authors.affiliation: University of Bergen, Dept of Biochemistry, Norway.
authors.forename: A J
authors.initials: AJ
authors.lastname: Raae
authors.forename: J
authors.initials: J
authors.lastname: Davenport
authors.forename: B
authors.initials: B
authors.lastname: Walther
mesh_terms: D000818:Animals; D002852:Chromatography, Ion Exchange; D005260:Female; D005399:Fishes / Q000378:metabolism*; D008970:Molecular Weight; D010053:Ovary / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology; D012697:Serine Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D011480:Protease Inhibitors; D012697:Serine Endopeptidases