A membrane-bound human placental protein kinase activated by endogenous polypeptides

Mossaad Abdel-Ghany; Shun Nakamura; Javier Navarro; Efraim Racker

doi:10.1007/BF01122460

A membrane-bound human placental protein kinase activated by endogenous polypeptides

Mossaad Abdel-Ghany, Shun Nakamura, Javier Navarro, Efraim Racker

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

A protein kinase (PPdPK) was purified from plasma membranes of human placenta. Phosphorylation of casein, but not of phosvitin or lactalbumin, by [γ-³²P]ATP in the presence of PPdPK was stimulated about 10-fold by naturally occurring polypeptides prepared from avariety of sources similar to the procedure of Roberts et al. (Proc. Natl. Acad. Sci. U.S.A. 77, 3494-3498, 1980). The amino acid phos-phorylated on casein was serine. According to gel exclusion chromatography the mol.wt, of PPdPK was 95 000. In autoradiograms, following polyacrylamide-gel electrophoresis, the autophosphorylation of PPdPK was greatly enhanced by the polypeptide activators.

Original language	English (US)
Pages (from-to)	275-282
Number of pages	8
Journal	Bioscience Reports
Volume	3
Issue number	3
DOIs	https://doi.org/10.1007/BF01122460
State	Published - Mar 1983
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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abstract = "A protein kinase (PPdPK) was purified from plasma membranes of human placenta. Phosphorylation of casein, but not of phosvitin or lactalbumin, by [γ-32P]ATP in the presence of PPdPK was stimulated about 10-fold by naturally occurring polypeptides prepared from avariety of sources similar to the procedure of Roberts et al. (Proc. Natl. Acad. Sci. U.S.A. 77, 3494-3498, 1980). The amino acid phos-phorylated on casein was serine. According to gel exclusion chromatography the mol.wt, of PPdPK was 95 000. In autoradiograms, following polyacrylamide-gel electrophoresis, the autophosphorylation of PPdPK was greatly enhanced by the polypeptide activators.",

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T1 - A membrane-bound human placental protein kinase activated by endogenous polypeptides

AU - Abdel-Ghany, Mossaad

AU - Nakamura, Shun

AU - Navarro, Javier

AU - Racker, Efraim

PY - 1983/3

Y1 - 1983/3

N2 - A protein kinase (PPdPK) was purified from plasma membranes of human placenta. Phosphorylation of casein, but not of phosvitin or lactalbumin, by [γ-32P]ATP in the presence of PPdPK was stimulated about 10-fold by naturally occurring polypeptides prepared from avariety of sources similar to the procedure of Roberts et al. (Proc. Natl. Acad. Sci. U.S.A. 77, 3494-3498, 1980). The amino acid phos-phorylated on casein was serine. According to gel exclusion chromatography the mol.wt, of PPdPK was 95 000. In autoradiograms, following polyacrylamide-gel electrophoresis, the autophosphorylation of PPdPK was greatly enhanced by the polypeptide activators.

AB - A protein kinase (PPdPK) was purified from plasma membranes of human placenta. Phosphorylation of casein, but not of phosvitin or lactalbumin, by [γ-32P]ATP in the presence of PPdPK was stimulated about 10-fold by naturally occurring polypeptides prepared from avariety of sources similar to the procedure of Roberts et al. (Proc. Natl. Acad. Sci. U.S.A. 77, 3494-3498, 1980). The amino acid phos-phorylated on casein was serine. According to gel exclusion chromatography the mol.wt, of PPdPK was 95 000. In autoradiograms, following polyacrylamide-gel electrophoresis, the autophosphorylation of PPdPK was greatly enhanced by the polypeptide activators.

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A membrane-bound human placental protein kinase activated by endogenous polypeptides

Abstract

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