Occurrence of a Novel 350-kDa Serine Proteinase in the Fluid of Porcine Ovarian Follicles and Its Increase during Their Maturation(Reproductive Biology)

概要

論文の詳細を見る
Porcine ovary was found to contain enzyme activities hydrolyzing peptide 4-methylcoumaryl-7-amide (MCA) substrates with a preference for Arg-MCA bond. The activities were shown to be present almost exclusively in the follicular fluid and to increase several times during follicular maturation. The enzyme responsible for these activities is thought to be a serine proteinase as judged from its strong inhibition by diisopropylfluorophosphate (DFP), leupeptin and antipain. The molecular weight of the native enzyme was electrophoretically estimated to be approximately 350,000, the result indicating that the enzyme is clearly distinct from plasmin (M_r=80,000) and collagenase (M_r=30,000-65,000), both of which are thought to be involved in ovulatory process. The substrate specificity of the partially purified enzyme was qualitatively different from that of plasmin. These results suggest that the enzyme is a novel type of serine proteinase.
社団法人日本動物学会の論文
1992-04-15