Premium
Phosphorylation of mitochondrial membrane proteins: effect of the surface potential on monoamine oxidase
Author(s) -
Famulski Konrad S.,
Nałȩcz Maciej J.,
Wojtczak Lech
Publication year - 1983
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(83)81129-6
Subject(s) - monoamine oxidase , chemistry , phosphorylation , mitochondrion , inner mitochondrial membrane , membrane , ethidium bromide , biochemistry , cytoplasm , membrane potential , biophysics , biology , enzyme , dna
Proteins of mitochondrial membranes become phosphorylated when liver mitochondria are incubated with ATP in the presence of Mg 2+ . This is accompanied by an increase of the negative surface potential of mitochondrial membranes, as calculated from the dissociation constant of fluorescent probes, 8‐anilino‐1‐naphthalene sulphonate and ethidium bromide, and by a decrease of the apparent K m ‐value of mitochondrial monoamine oxidase. Protein phosphorylation, the increase of the negative surface potential and the decrease of apparent K m of monoamine oxidase are greatly potentiated by cytoplasmic protein kinases in the presence of cyclic AMP.