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Collagenase induced changes in the circular dichroism spectrum of collagen

✍ Scribed by F. H. Chu; A. Lukton


Publisher
Wiley (John Wiley & Sons)
Year
1974
Tongue
English
Weight
356 KB
Volume
13
Category
Article
ISSN
0006-3525

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✦ Synopsis


The maximum at 220 nm in the circular dichroism spectrum of native collagen solution changed to a negative value after heat denaturation or collagenase hydrolysis. The enzyme induced rate of C1) change a t 220 nm was shown to be first order in collagen concentration. The specific rate constant k is actually a combined rate constant kfast and k,l,,v in which the ratio k,/k, is 4.1. The initial rates were linear with respect t o enzyme concentration, and the I<, was found to be 3.5 X 10-7 Ill. The rate of ultraviolet hyperchromicity at 220 nm on collagen hydrolysis was determined. The kf3't was the same as that obtained by C1).

Both methods may be readily wed to assay for collagenase activity.

The k,/k, ratio was 4.6.


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