Elsevier

Experimental Eye Research

Volume 25, Issue 5, November 1977, Pages 435-445
Experimental Eye Research

Latent collagenase in the ulcerating rabbit cornea

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Abstract

“Latent” collagenase has been activated by brief trypsin treatment of crude culture media protein from both ulcerating and non-ulcerating (normal) rabbit corneas. Collagenase activity generated in this way is able to cleave re-constituted collagen in fibrils and cleaves soluble collagen into 34- and 14-length fragments in the manner of the vertebrate collagenases. Collagenase activity has been generated also by trypsin treatment of molecular sieve fractions containing protein only slightly larger in size than the manifest collagenase of approximately 40 000 mol weight. Both latent and manifest collagenase treated with trypsin elute with an apparent molecular weight of 23 000 and are capable of being bound by the serum antiprotease, α2-macroglobulin. The nature of the latent collagenase is not known. It may be a complex of collagenase with an inhibitor, or it may be a zymogen.

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  • Cited by (0)

    “Latent” collagenase is defined here as inactive collagenase that is made active by treatment with trypsin. “Manifest” collagenase is defined as collagenase which is active without prior trypsin treatment. “Total collagenase” activity is the sum of activity due to manifest collagenase plus collagenase activity that is due to trypsin activation of latent collagenase.

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