Kinetic analysis of the binding of human matrix metalloproteinase-2 and-9 to tissue inhibitor of metalloproteinase (TIMP)-1 and TIMP-2
MW Olson, DC Gervasi, S Mobashery… - Journal of Biological …, 1997 - ASBMB
The dissociation constants (K d) of tissue inhibitor of metalloproteinase (TIMP)-1 and TIMP-2
for the active and latent forms of matrix metalloproteinase (MMP)-2 and MMP-9 were
evaluated using surface plasmon resonance (SPR) and enzyme inhibition studies. SPR
analysis shows biphasic kinetics with high (nm) and low (μm) affinity binding sites of TIMP-2
and TIMP-1 for MMP-2 (72-and 62-kDa species) and MMP-9 (92-and 82-kDa species),
respectively. In contrast, binding data of TIMP-2 to an MMP-2 45-kDa active form lacking the …
for the active and latent forms of matrix metalloproteinase (MMP)-2 and MMP-9 were
evaluated using surface plasmon resonance (SPR) and enzyme inhibition studies. SPR
analysis shows biphasic kinetics with high (nm) and low (μm) affinity binding sites of TIMP-2
and TIMP-1 for MMP-2 (72-and 62-kDa species) and MMP-9 (92-and 82-kDa species),
respectively. In contrast, binding data of TIMP-2 to an MMP-2 45-kDa active form lacking the …
