Characteristics of a proteinase from ovarian fluid of the lumpsucker (Cyclopterus lumpus L.) |
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Authors: | A J Raae J Davenport B Walther |
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Affiliation: | University of Bergen, Dept of Biochemistry, Norway. |
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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. |
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