A high molecular weight collagenase inhibitor made by rabbit chondrocytes in cell culture.
A new, high molecular weight (66,000 daltons) inhibitor of collagenase (LCI) has been isolated and partially characterized. It accounted for 20% of the collagenase-inhibitory activity in the supernatants of rabbit chondrocytes cultured in 10% acid-treated fetal bovine serum (ATFBS). LCI was stable to 60 degrees C and sensitive to reduction and alkylation. Unlike a low molecular weight collagenase inhibitor, similar to Tissue Inhibitor of Metallo-Proteinases (TIMP), it did not bind to concanavalin A-Sepharose 4B.
Morris
G M
GM
Department of Pharmacology, State University of New York, Stony Brook 11794-8651.
D000818:Animals; D002356:Cartilage / Q000166:cytology / Q000201:enzymology*; D002478:Cells, Cultured; D004791:Enzyme Inhibitors / Q000302:isolation & purification*; D003012:Microbial Collagenase / Q000378:metabolism*; D008970:Molecular Weight; D011817:Rabbits
D004791:Enzyme Inhibitors; D003012:Microbial Collagenase