Absence of phosphorylation of retinoid-binding proteins by protein kinase C in vitro

Mitsuo Ninomiya, Hirota Fujiki, Nam Sun Paik, Takahiko Horiuchi, R. K. Boutwell

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

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).

Original languageEnglish
Pages (from-to)330-334
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume138
Issue number1
DOIs
Publication statusPublished - Jul 16 1986
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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