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Collagenase induced changes in the circular dichroism spectrum of collagen
Author(s) -
Chu F. H.,
Lukton A.
Publication year - 1974
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1974.360130713
Subject(s) - chemistry , circular dichroism , collagenase , hyperchromicity , reaction rate constant , hydrolysis , enzyme , denaturation (fissile materials) , analytical chemistry (journal) , crystallography , chromatography , nuclear chemistry , kinetics , biochemistry , dna , physics , quantum mechanics
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 CD change at 220 nm was shown to be first order in collagen concentration. The specific rate constant k is actually a combined rate constant k fast and k slow in which the ratio k f / k s is 4.1. The initial rates were linear with respect to enzyme concentration, and the K m was found to be 5.5 × 10 −7 M . The rate of ultraviolet hyperchromicity at 220 nm on collagen hydrolysis was determined. The k fast was the same as that obtained by CD. The k f / k s ratio was 4.6. Both methods may be readily used to assay for collagenase activity.