Multi‐site phosphorylation in ox‐kidney branched‐chain 2‐oxoacid dehydrogenase complex
- 22 August 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 160 (1-2) , 149-152
- https://doi.org/10.1016/0014-5793(83)80955-7
Abstract
Tryptic [32P]phosphopeptides were prepared from [32P]phosphorylated ox-kidney branched-chain complex and analysed by high-voltage paper electrophoresis at pH 1.9. In the maximally phosphorylated complex 3 tryptic [32P]phosphopeptides were identified (TA, TB, TC). R F-values relative to N 6-dinitrophenyllysine were (mean ± SEM for 25 obs.): TA, 1.53 ± 0.03; TB, 1.07 ± 0.02; TC, 0.65 ± 0.01. Relative rates of phosphorylation were TA > TB > TC. Phosphorylation of TA reached a maximum when about 66% of the complex was inactivated. Phosphorylation of TB and TC was associated mainly with 66–95% inactivation of the complex.Keywords
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