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

doi:10.1016/0006-291X(86)90284-6

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 journal › Article › peer-review

5 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 language	English
Pages (from-to)	330-334
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	138
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(86)90284-6
Publication status	Published - Jul 16 1986
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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

Cite this

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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.\}",

note = "Funding Information: This work was supported in part by Grants-in-Aid for Cancer Research from the Ministry of Education, Science and Culture and the Ministry of Health and Welfare for a Comprehensive IO-year Strategy of Cancer Cocitrol, Japan and by a grant from the Princess Takamatsu Cancer Research Fund. Mitsuo Ninomiya and Nam Sun Paik thank the Foundation for Promotion of Cancer Research, Japan for support of their work at the National Cancer Center Research Institute, Tokyo.",

year = "1986",

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doi = "10.1016/0006-291X(86)90284-6",

language = "English",

volume = "138",

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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.

N1 - Funding Information: This work was supported in part by Grants-in-Aid for Cancer Research from the Ministry of Education, Science and Culture and the Ministry of Health and Welfare for a Comprehensive IO-year Strategy of Cancer Cocitrol, Japan and by a grant from the Princess Takamatsu Cancer Research Fund. Mitsuo Ninomiya and Nam Sun Paik thank the Foundation for Promotion of Cancer Research, Japan for support of their work at the National Cancer Center Research Institute, Tokyo.

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).

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JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

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

Abstract

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