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Quantitative study of the binding of cysteine proteinases to basement membranes
Author(s) -
Guinec N.,
Dalet-Fumeron V.,
Pagano M.
Publication year - 1992
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(92)81299-2
Subject(s) - papain , cysteine , chemistry , cathepsin , enzyme , basement membrane , biochemistry , membrane , cathepsin l , superfamily , biology , microbiology and biotechnology , receptor
Binding of cysteine proteinases of the papain superfamily (papain and cathepsins B, B‐like and L) to basement membranes was studied by using the enzymatic activity of these proteinases against their specific fluorogenic substrates. Papain inactived by E64 was used for K d determination by competition experiments. The binding was characterized using the following parameters, the equilibrium constant, K d , and the number of substract sites, n , values of which were in the range of 10 −7 and 10 12 , respectively. Such results would be of significant interest for the understanding of the biological role of cysteine proteinases in tumour invasion and other types of tissue remodeling.