Proteases in the Emory mouse cataract.

Abstract

Exopeptidases identified as dipeptidyl peptidase III and leucine aminopeptidase, and an endopeptidase, prolyl endopeptidase, were found in the Emory Mouse cataract and the Cataract Resistant mouse lens extracts. The specific activity measured on Arg-Arg-2-NNap for DPP III and the hydrolysis of Boc-Arg-Pro-2-NNap for prolyl endopeptidase were higher in the Emory Mouse cataractous lens extract. A relatively high rate of hydrolysis of the beta-naphthylamide of leucine aminopeptidase was present in both mouse categories; however, the Cataract Resistant mouse lens had approximately double the protease activity of the Emory Mouse cataract.

• Authors: A A Swanson, R M Davis, N C Meinhardt, K D Kuck, J F Kuck Jr
• Journal: Investigative ophthalmology & visual science (Invest Ophthalmol Vis Sci) Vol. 26 Issue 7 Pg. 1035-7 (Jul 1985) ISSN: 0146-0404 [Print] United States
• PMID: 3891668 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Exopeptidases
• Peptide Hydrolases

Topics

• Animals
• Cataract (enzymology)
• Exopeptidases
• Lens, Crystalline (enzymology)
• Mice
• Mice, Inbred Strains
• Peptide Hydrolases (metabolism)