AVIS-IBIS

Birds of Indian Subcontinent

Occurrence of a Latent Serine Protease in the Follicular Fluid of Porcine Ovary

Publication Type:Journal Article
Year of Publication:1995
Authors:Ohnishi, J, Takahashi, T
Journal:Zoological Science
Volume:12
Issue:1
Date Published:1995
ISBN Number:0289-0003
Keywords:Fringillidae, Serinus, Serinus serinus
Abstract:Abstract Porcine ovary folliclular fluid contains a latent form of a protease which is activatable with trypsin. The active enzyme hydrolyzed peptide 4-methylcoumaryl-7-amide (MCA) substrates with a preference for the Arg-MCA bond. The enzyme was strongly inhibited by diisopropylfluorophosphatc, aprotinin, leupeptin and antipain, but not by soybean trypsin inhibitor. The apparent molecular weight of the enzyme was approximately 630,000 as estimated by gel filtration. No significant difference in molecular size was seen between the inactive precursor and trypsin-activated enzyme. The results suggest that the present enzyme is a novel type of serine protease.Abstract Porcine ovary folliclular fluid contains a latent form of a protease which is activatable with trypsin. The active enzyme hydrolyzed peptide 4-methylcoumaryl-7-amide (MCA) substrates with a preference for the Arg-MCA bond. The enzyme was strongly inhibited by diisopropylfluorophosphatc, aprotinin, leupeptin and antipain, but not by soybean trypsin inhibitor. The apparent molecular weight of the enzyme was approximately 630,000 as estimated by gel filtration. No significant difference in molecular size was seen between the inactive precursor and trypsin-activated enzyme. The results suggest that the present enzyme is a novel type of serine protease.
URL:http://dx.doi.org/10.2108/zsj.12.87
Short Title:Zoological Science
Scratchpads developed and conceived by (alphabetical): Ed Baker, Katherine Bouton Alice Heaton Dimitris Koureas, Laurence Livermore, Dave Roberts, Simon Rycroft, Ben Scott, Vince Smith