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pubmed-article:3017322pubmed:abstractTextCellular 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).lld:pubmed
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pubmed-article:3017322pubmed:articleTitleAbsence of phosphorylation of retinoid-binding proteins by protein kinase C in vitro.lld:pubmed
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