| Literature DB >> 6884504 |
K S Lau, C E Phillips, P J Randle.
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). RF-values relative to N6-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 greater than TB greater than 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.Entities:
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Year: 1983 PMID： 6884504 DOI： 10.1016/0014-5793(83)80955-7
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124