Abstract
A chondromucoprotease present in bovine cartilage, with optimal activity at pH 5, has been partially characterized. This autolytic enzyme was irreversibly inhibited by chloroquine, those of its metabolites with a quinoline nucleus, and mepacrine (quinacrine, atebrine). These drugs did not affect cartilage degradation by a mucopolysaccharase (ovine hyaluronidase) or papain. At relatively high concentrations (10 mM), chloroquine and some of its metabolites inhibited rat skin collagenase, a presumed collagenase in bovine cartilage and a bacterial collagenase (clostridiopeptidase A). This drug action was reversible and non-competitive with the substrate, when this was gelatine. Rivanol and acetyl ammonium salts (0·25 mM) were powerful inhibitors of clostridiopeptidase A. Other types of anti-inflammatory (antirheumatic) drugs did not inhibit either the chondromucoprotease or the collagenases. A neutral sulphydryl-dependent esterase in bovine nasal cartilage was inhibited high levels of chloroquine. Chloroquine and hydroxychloroquine were metabolised (de-ethylated) by bovine cartilage incubated at pH 7·4. The possible value of (a) chloroquine and mepacrine for treating degenerative arthritis, and of (b) cetyl ammonium salts for treating clostridial infections, is discussed.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
