Dissociation of tissue inhibitor of metalloproteinases (TIMP) from enzyme complexes yields fully active inhibitor.
Recombinant human tissue inhibitor of metalloproteinases (TIMP) forms complexes with high-Mr active recombinant stromelysin that are stable over long periods under physiological conditions. TIMP-stromelysin complexes could be dissociated in the presence of EDTA at pH 3, releasing free TIMP and destroying stromelysin activity. The dissociated TIMP was apparently unmodified, in contrast with other known protein inhibitors of metalloproteinases and many classes of serine-proteinase inhibitor, which are slowly cleaved.
Murphy
G
G
Strangeways Research Laboratory, Cambridge, U.K.
Koklitis
P
P
Carne
A F
AF
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D004791:Enzyme Inhibitors / Q000378:metabolism*; D006801:Humans; D019278:Matrix Metalloproteinase 3; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors*; D008969:Molecular Sequence Data; D019714:Tissue Inhibitor of Metalloproteinases
D004791:Enzyme Inhibitors; D019714:Tissue Inhibitor of Metalloproteinases; D008666:Metalloendopeptidases; D019278:Matrix Metalloproteinase 3