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Preferential binding of collagenase to α 2 ‐macroglobulin in the presence of the tissue inhibitor of metalloproteinases
Author(s) -
Cawston Timothy E.,
Mercer Elizabeth
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81074-2
Subject(s) - collagenase , matrix metalloproteinase , chemistry , macroglobulin , microbial collagenase , biochemistry , enzyme , metalloproteinase , cleavage (geology) , interstitial collagenase , binding site , microbiology and biotechnology , biology , paleontology , fracture (geology)
The binding of collagenase to both α2‐niacroglobulin and the tissue inhibitor of metalloproteinases was studied using purified materials. Collagenase bound preferentially to α 2 ‐macroglobulin although no transfer of collagenase to α 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.