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Studies on the cathepsins in elastic cartilage.


ABSTRACT: 1. The presence of several enzymes in rabbit ear cartilage was examined by a quantitative method that permits the incubation of a fixed weight of cartilage sections (18mum.) with an appropriate exogeneous substrate. 2. As the presence of cathepsins B and D in cartilage has already been established, evidence is now provided to show that cathepsins A and C are also present and are maximally active at pH5. 3. Cathepsin A was recognized by its hydrolysis of benzyloxycarbonyl-glutamyl-tyrosine and cathepsin C by its hydrolysis of glycyl-tyrosine amide; the cartilage also hydrolysed benzyloxycarbonyl-glutamyl-phenylalanine and benzoyl-dl-phenylalanine 2-naphthyl ester at pH5. 4. The acid phosphatase activity and the DNA content of cartilage have also been measured to provide a basis for comparison with the cathepsin activity of cartilage obtained from other sites and species.

SUBMITTER: Ali SY 

PROVIDER: S-EPMC1187730 | biostudies-other | 1969 May

REPOSITORIES: biostudies-other

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