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Multi‐site phosphorylation of branched‐chain 2‐oxoacid dehydrogenase complex within mitochondria isolated from rat liver, kidney and heart
Author(s) -
Cook Kenneth G.,
Lawson Rowena,
Yeaman Stephen J.
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)80024-6
Subject(s) - phosphorylation , protein subunit , mitochondrion , biochemistry , chemistry , succinate dehydrogenase , in vitro , biology , microbiology and biotechnology , gene
The α subunit of the E 1 component of branched‐chain 2‐oxoacid dehydrogenase complex becomes rapidly phosphorylated in rat liver, kidney and heart mitochondria incubated in the presence of succinate and [ 32 P]phosphate. Peptide mapping of tryptic digests of the phosphorylated α subunit indicates that 3 distinct sites are phosphorylated, as has been reported previously by us for phosphorylation in vitro of highly purified complex.