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

5 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

Access to Document

10.1007/BF01122460

Cite this

@article{e4abd7952a034cf8a601d23b13bf766f,

title = "A membrane-bound human placental protein kinase activated by endogenous polypeptides",

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.",

author = "Mossaad Abdel-Ghany and Shun Nakamura and Javier Navarro and Efraim Racker",

year = "1983",

month = mar,

doi = "10.1007/BF01122460",

language = "English (US)",

volume = "3",

pages = "275--282",

journal = "Bioscience Reports",

issn = "0144-8463",

publisher = "Portland Press Ltd.",

number = "3",

}

TY - JOUR

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.

UR - http://www.scopus.com/inward/record.url?scp=0020530642&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020530642&partnerID=8YFLogxK

U2 - 10.1007/BF01122460

DO - 10.1007/BF01122460

M3 - Article

C2 - 6860786

AN - SCOPUS:0020530642

SN - 0144-8463

VL - 3

SP - 275

EP - 282

JO - Bioscience Reports

JF - Bioscience Reports

IS - 3

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this