-transparent.png){kind=logo}
A new method for the assay of collagenase activity has been developed, whereby the collagen cleavage products, after initial collagenase digestion, are degraded further by a mixture of trypsin and alpha-chymotrypsin. The degradation products are soluble in TCA and can be conveniently separated from the remaining uncleaved collagen substrate by rapid filtration. The enzyme assay is shown to be reproducible and sensitive, and it lends itself to a convenient and rapid determination of collagenase activity in relatively large numbers of samples. The applicability of this method is demonstrated by the detection of increased collagenase activity in skin fibroblast cultures derived from a patient with recessive dystrophic epidermolysis bullosa.
L Ryhänen, and
S Rantala-Ryhänen, and
E M Tan, and
J Uitto
September 1975,
Analytical biochemistry,
L Ryhänen, and
S Rantala-Ryhänen, and
E M Tan, and
J Uitto
July 1981,
Journal of periodontal research,
L Ryhänen, and
S Rantala-Ryhänen, and
E M Tan, and
J Uitto
October 1976,
Biochimica et biophysica acta,
L Ryhänen, and
S Rantala-Ryhänen, and
E M Tan, and
J Uitto
June 2003,
Biotechnology and applied biochemistry,
L Ryhänen, and
S Rantala-Ryhänen, and
E M Tan, and
J Uitto
January 2017,
Methods in molecular biology (Clifton, N.J.),
L Ryhänen, and
S Rantala-Ryhänen, and
E M Tan, and
J Uitto
April 2008,
Electrophoresis,
L Ryhänen, and
S Rantala-Ryhänen, and
E M Tan, and
J Uitto
November 1979,
Analytical biochemistry,
L Ryhänen, and
S Rantala-Ryhänen, and
E M Tan, and
J Uitto
May 1976,
Analytical biochemistry,
L Ryhänen, and
S Rantala-Ryhänen, and
E M Tan, and
J Uitto
January 1980,
The Kurume medical journal,
L Ryhänen, and
S Rantala-Ryhänen, and
E M Tan, and
J Uitto
September 1983,
Analytical biochemistry,
