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Binding of Chlorpromazine to S‐100 Protein
Author(s) -
Donato Rosario
Publication year - 1984
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1984.tb02811.x
Subject(s) - egta , chlorpromazine , chemistry , titratable acid , binding site , stereochemistry , calcium , biochemistry , endocrinology , biology , organic chemistry
Chlorpromazine (CPZ) induces in S‐100 conformational changes resulting in the exposure of titratable SH groups of the protein to the solvent. This effect is even greater in the presence of Mg 2+ ± Ca 2+ . S‐100 possesses binding sites for CPZ. The binding of CPZ to 3 μ M S‐100 is half‐saturated by 0.18 μ M CPZ in the presence of Mg 2+ plus Ca 2+ and by 0.24 μ M CPZ in the presence of Mg 2+ plus EGTA. The extent of the binding is greater in the presence of Ca 2+ than in the presence of EGTA, especially at low CPZ concentrations.