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α 2 High molecular mass cysteine proteinase inhibitor: HMrα 2 ‐CPI
Author(s) -
Pagano M.,
Engler R.
Publication year - 1984
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(84)80045-9
Subject(s) - proteinase inhibitor , cathepsin , chemistry , cathepsin d , dissociation constant , cysteine , enzyme , reaction rate constant , biochemistry , cathepsin l , cathepsin o , microbiology and biotechnology , biology , kinetics , physics , receptor , quantum mechanics
HMrα 2 CPI was found to be an inhibitor of human liver cathepsin H by the measurement of the dissociation constant ( K i ), the association rate constant ( k 1 ) and the dissociation rate constant ( k −1 ) between the enzyme and the inhibitor. These data suggest that this protein‐proteinase inhibitor can play a physiological role in the regulation of free cathepsin H.