Separation and partial characterization of three forms of collagenase inhibitor from bovine gingiva.
Three forms of collagenase inhibitor were isolated; one bound to Con A-Sepharose and the other two did not. The Con A-bound (Mr 38,000) and the two unbound (Mr 50,000 and 22,000) inhibitors contained about 20, 15 and 65% of the total inhibitory activity, respectively. The bound and one of the unbound (Mr 22,000) inhibitors were fairly specific for mammalian collagenase; the other unbound inhibitor was rather non-specific and also inhibited trypsin and thermolysin, but not bacterial collagenase. All the inhibitors were heat stable (90 degrees C, 30 min) and unaffected by 4-aminophenylmercuric acetate, but were inactivated by reduction and alkylation.
Adachi
Y
Y
Department of Biochemistry, Niigata University School of Dentistry, Japan.
Nohara
H
H
D000818:Animals; D002417:Cattle; D005591:Chemical Fractionation; D002850:Chromatography, Gel; D005881:Gingiva / Q000201:enzymology*; D003012:Microbial Collagenase / Q000037:antagonists & inhibitors*
D003012:Microbial Collagenase