Preferential binding of collagenase to alpha 2-macroglobulin in the presence of the tissue inhibitor of metalloproteinases.
The binding of collagenase to both alpha 2-macroglobulin and the tissue inhibitor of metalloproteinases was studied using purified materials. Collagenase bound preferentially to alpha 2-macroglobulin although no transfer of collagenase to alpha 2-macroglobulin occurred if the enzyme was first mixed with the tissue inhibitor of metalloproteinases. The sequences of amino acids in both inhibitors likely to be responsible for the binding of collagenase are discussed and compared to the cleavage site in the collagen molecule.
D000818:Animals; D010450:Endopeptidases; D004791:Enzyme Inhibitors / Q000502:physiology*; D008666:Metalloendopeptidases; D003012:Microbial Collagenase / Q000378:metabolism*; D008970:Molecular Weight; D011480:Protease Inhibitors; D011485:Protein Binding; D013552:Swine; D019714:Tissue Inhibitor of Metalloproteinases; D000511:alpha-Macroglobulins / Q000378:metabolism*
D004791:Enzyme Inhibitors; D011480:Protease Inhibitors; D019714:Tissue Inhibitor of Metalloproteinases; D000511:alpha-Macroglobulins; D010450:Endopeptidases; D008666:Metalloendopeptidases; D003012:Microbial Collagenase