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- W2171917465 abstract "Abstract: A fraction of chromaffin granule membranes contained a number of substrates for endogenous protein kinase activity as well as endogenous phosphatase activity. The major 32P-labelled polypeptide of molecular weight 43,000 appeared to be the α-subunit of pyruvate dehydrogenase of residual mitochondria. Several polypeptides showed cyclic AMP stimulation of phosphorylation of which the major polypeptide of molecular weight 59,000 shows half-maximal phosphorylation with 0.49 μM cyclic AMP. The phosphorylation of several other polypeptides is inhibited at high cyclic AMP concentrations. From studies with immunoprecipitation and two-dimensional electrophoresis it was found that α- and β-tubulin and actin were absent from the granule membranes. However 32P labelling of a proportion of the copies of dopamine-β-hydroxylase was demonstrated. The majority of the substrates for endogenous protein kinase activity are probably on the cytoplasmic side of the granule membrane." @default.
- W2171917465 created "2016-06-24" @default.
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- W2171917465 date "1982-11-01" @default.
- W2171917465 modified "2023-10-16" @default.
- W2171917465 title "Phosphoproteins of the Adrenal Chromaffin Granule Membrane" @default.
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- W2171917465 doi "https://doi.org/10.1111/j.1471-4159.1982.tb12582.x" @default.
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