Absence of phosphorylation of retinoid-binding proteins by protein kinase C in vitro.
Cellular retinol-binding protein, cellular retinoic acid-binding protein, and fetal cellular retinol-binding protein were purified to homogeneity and each polypeptide had a molecular weight of 16,000. Their apoproteins were not phosphorylated under the same conditions. Their holoproteins did not inhibit the phosphorylation of histone III-S by protein kinase C. Each of these observations is contrary to the results reported by Cope et al. (Biochem. Biophys. Res. Commun., 120, 593-601, 1984).
D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D018168:Receptors, Retinoic Acid; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D013997:Time Factors
D002352:Carrier Proteins; D018168:Receptors, Retinoic Acid; D011493:Protein Kinase C