Acidic lens protein degrading activity in bovine ciliary body.
Biochemical studies of acidic lens protein degrading activity in the bovine ciliary body were performed. The activity showed two peaks, Fractions A and B, on Sephadex G-75 column chromatography. Fraction A contained cathepsin D and thiol proteinase activities and was inhibited by pepstatin and leupeptin. Fraction B contained thiol proteinase activity and was inhibited by leupeptin. The proportion of peptide released from the lens protein by Fractions A and B was higher than those from bovine serum albumin and casein. Lens protein may be a good assay substrate for cathepsin D and lysosomal thiol proteinase in the ciliary body.
D000818:Animals; D002417:Cattle; D002845:Chromatography; D002924:Ciliary Body / Q000378:metabolism*; D003459:Crystallins / Q000378:metabolism*; D003545:Cysteine / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007976:Leupeptins / Q000494:pharmacology; D010436:Pepstatins / Q000494:pharmacology; D011480:Protease Inhibitors
D003459:Crystallins; D007976:Leupeptins; D010436:Pepstatins; D011480:Protease Inhibitors; C014195:Streptomyces pepsin inhibitor; C032854:leupeptin; D003545:Cysteine; C031375:pepstatin