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A rapid assay method for vertebrate collagenase (EC 3.4.24.3) activity has been developed using 14C-labeled soluble collagen as substrate. The method is based on the incubation of collagen with enzyme in the presence of glucose to prevent collagen fibril formation followed by selective extraction of the enzyme digestion products into dioxane at a final concentration of 50%. The rate of reaction was about 10 times higher than that obtained by the conventional method using reconstituted collagen fibrils as substrate and the relationship between enzyme activity and concentration was linear over a wider range. When the method was applied to the assay of human granulocyte collagenase, the results showed good correlation with those obtained by the conventional gel method.
K Terato, and
Y Nagai, and
K Kawanishi, and
S Yamamoto
January 1980,
The Kurume medical journal,
K Terato, and
Y Nagai, and
K Kawanishi, and
S Yamamoto
May 1984,
Analytical biochemistry,
K Terato, and
Y Nagai, and
K Kawanishi, and
S Yamamoto
November 1979,
Analytical biochemistry,
K Terato, and
Y Nagai, and
K Kawanishi, and
S Yamamoto
January 1989,
Analytical biochemistry,
K Terato, and
Y Nagai, and
K Kawanishi, and
S Yamamoto
January 2005,
Biomeditsinskaia khimiia,
K Terato, and
Y Nagai, and
K Kawanishi, and
S Yamamoto
January 1977,
Zeitschrift fur Rheumatologie,
K Terato, and
Y Nagai, and
K Kawanishi, and
S Yamamoto
September 1969,
Analytical biochemistry,
K Terato, and
Y Nagai, and
K Kawanishi, and
S Yamamoto
November 1980,
Analytical biochemistry,
K Terato, and
Y Nagai, and
K Kawanishi, and
S Yamamoto
June 1980,
Journal of biochemistry,
K Terato, and
Y Nagai, and
K Kawanishi, and
S Yamamoto
July 1971,
Analytical biochemistry,
