Properties of a collagenase inhibitor partially purified from cultures of smooth muscle cells.
An inhibitor of mammalian collagenase has been partially purified from the spent medium of smooth muscle cells grown in culture. The inhibitor is a glycoprotein with an apparent molecular weight of 25,000. It is stable to heat, acid, and mercurials, but is destroyed by trypsin treatment and by reductive alkylation. The inhibitor interacts with active mammalian collagenase and this interaction results in the loss of enzymatic activity. This presumptive collagenase-inhibitor complex is stable to the treatment with mercurials and to trypsin. These latter observations suggest that this inhibitor is different from other collagenase inhibitors that are thought to be responsible for the latency of the enzyme.
D000818:Animals; D001011:Aorta / Q000032:analysis; D004355:Drug Stability; D005347:Fibroblasts / Q000201:enzymology; D006023:Glycoproteins / Q000302:isolation & purification* / Q000494:pharmacology; D006358:Hot Temperature; D003012:Microbial Collagenase / Q000037:antagonists & inhibitors*; D008970:Molecular Weight; D009130:Muscle, Smooth / Q000032:analysis*; D013552:Swine
D006023:Glycoproteins; D003012:Microbial Collagenase