Abstract
Phosphorylation of specific proteins in subcellular fractions of rat brain is affected by the presence of low concentrations (1–50 μM) of triethyltin bromide (Et 3SnBr), in vitro. SDS-PAGE and autoradiography showed that Et 3SnBr increased phosphorylation of an M r = 42,000 protein and an M r = 76,000–80,000 doublet band, but decreased phosphorylation of an M r = 52,000 component. The M r = 42,000 and 76,000–80,000 phosphoproteins have been identified as the α-subunit of pyruvate dehydrogenase (PDH) and synapsin, respectively. Et 3SnBr-induced phosphorylation of rabbit brain PDH results in partial inactivation of the PDH complex.
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