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 journalArticle

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

Fingerprint

Cellular Retinol-Binding Proteins
Retinol-Binding Proteins
Phosphorylation
Protein Kinase C
Fetal Proteins
Retinoic Acid Receptors
Apoproteins
Histones
Molecular Weight
Molecular weight
Peptides
In Vitro Techniques

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Absence of phosphorylation of retinoid-binding proteins by protein kinase C in vitro. / Ninomiya, Mitsuo; Fujiki, Hirota; Paik, Nam Sun; Horiuchi, Takahiko; Boutwell, R. K.

In: Biochemical and Biophysical Research Communications, Vol. 138, No. 1, 16.07.1986, p. 330-334.

Research output: Contribution to journalArticle

Ninomiya, Mitsuo ; Fujiki, Hirota ; Paik, Nam Sun ; Horiuchi, Takahiko ; Boutwell, R. K. / Absence of phosphorylation of retinoid-binding proteins by protein kinase C in vitro. In: Biochemical and Biophysical Research Communications. 1986 ; Vol. 138, No. 1. pp. 330-334.
@article{ec42e3f8df78491391f98874eea54cab,
title = "Absence of phosphorylation of retinoid-binding proteins by protein kinase C in vitro",
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).",
author = "Mitsuo Ninomiya and Hirota Fujiki and Paik, {Nam Sun} and Takahiko Horiuchi and Boutwell, {R. K.}",
year = "1986",
month = "7",
day = "16",
doi = "10.1016/0006-291X(86)90284-6",
language = "English",
volume = "138",
pages = "330--334",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Absence of phosphorylation of retinoid-binding proteins by protein kinase C in vitro

AU - Ninomiya, Mitsuo

AU - Fujiki, Hirota

AU - Paik, Nam Sun

AU - Horiuchi, Takahiko

AU - Boutwell, R. K.

PY - 1986/7/16

Y1 - 1986/7/16

N2 - 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).

AB - 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).

UR - http://www.scopus.com/inward/record.url?scp=0022444012&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022444012&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(86)90284-6

DO - 10.1016/0006-291X(86)90284-6

M3 - Article

C2 - 3017322

AN - SCOPUS:0022444012

VL - 138

SP - 330

EP - 334

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -