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Phosphorylation of filamin and other proteins in cultured fibroblasts.
Authors:P Davies  Y Shizuta  K Olden  M Gallo  I Pastan
Affiliation:National Institutes of Health National Cancer Institute Laboratory of Molecular Biology Bethesda, Maryland 20014 USA
Abstract:Incubation of subcellular fractions of fibroblasts with [32P]ATP demonstrated 10 phosphoproteins whose phosphorylation can be increased by cyclic AMP or cyclic AMP-dependent protein kinase. One of these phosphoproteins, MW 240,000, resembles the actin binding protein, filamin, and can be selectively precipitated by antibodies to chicken gizzard filamin. Furthermore chicken gizzard filamin can be phosphorylated by skeletal muscle protein kinase and cyclic AMP stimulates this reaction.
Keywords:cyclic AMP  adenosine 3′:5′-cyclic monophosphate  EGTA  ethylene glycol bis(β-aminoethylether)-N,N′-tetraacetic acid  MES  2-(N-morpholino)ethanesulfonic acid  SDS  sodium dodecyl sulfate  NRK  normal rat kidney fibroblasts
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