Nucleolin (C23), a physiological substrate for casein kinase II

H R Schneider, O G Issinger

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Nucleolin (C23), a 110 kDa phosphoprotein, which is mainly found in the nucleolus has been shown to be a physiological substrate for casein kinase II (CKII). Nucleolin was identified and characterized by immunodetection using an anti-nucleolin antibody. Phosphopeptide patterns from nucleolin phosphorylated by purified casein kinase II and of phosphorylated nucleolin which had been isolated from tumor cells grown in the presence of [32P]-o-phosphate, were identical. The partial tryptic digest revealed nine phosphopeptides. Nucleolin isolated from Krebs II mouse ascites cells was phosphorylated by purified casein kinase II with about two moles phosphate per one mole of nucleolin.
Original languageEnglish
JournalBiochemical and Biophysical Research Communications
Volume156
Issue number3
Pages (from-to)1390-1397
Number of pages7
ISSN0006-291X
Publication statusPublished - 15. Nov 1988

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Casein Kinase II
Substrates
Phosphopeptides
Phosphates
Phosphoproteins
phosphoprotein C23
nucleolin
Tumors
Cells
Antibodies
Neoplasms

Keywords

  • Animals
  • Carcinoma, Ehrlich Tumor
  • Casein Kinases
  • Mice
  • Nuclear Proteins
  • Phosphoproteins
  • Phosphorylation
  • Protein Kinases
  • RNA-Binding Proteins

Cite this

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title = "Nucleolin (C23), a physiological substrate for casein kinase II",
abstract = "Nucleolin (C23), a 110 kDa phosphoprotein, which is mainly found in the nucleolus has been shown to be a physiological substrate for casein kinase II (CKII). Nucleolin was identified and characterized by immunodetection using an anti-nucleolin antibody. Phosphopeptide patterns from nucleolin phosphorylated by purified casein kinase II and of phosphorylated nucleolin which had been isolated from tumor cells grown in the presence of [32P]-o-phosphate, were identical. The partial tryptic digest revealed nine phosphopeptides. Nucleolin isolated from Krebs II mouse ascites cells was phosphorylated by purified casein kinase II with about two moles phosphate per one mole of nucleolin.",
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pages = "1390--1397",
journal = "Biochemical and Biophysical Research Communications",
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Nucleolin (C23), a physiological substrate for casein kinase II. / Schneider, H R; Issinger, O G.

In: Biochemical and Biophysical Research Communications, Vol. 156, No. 3, 15.11.1988, p. 1390-1397.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - Nucleolin (C23), a physiological substrate for casein kinase II

AU - Schneider, H R

AU - Issinger, O G

PY - 1988/11/15

Y1 - 1988/11/15

N2 - Nucleolin (C23), a 110 kDa phosphoprotein, which is mainly found in the nucleolus has been shown to be a physiological substrate for casein kinase II (CKII). Nucleolin was identified and characterized by immunodetection using an anti-nucleolin antibody. Phosphopeptide patterns from nucleolin phosphorylated by purified casein kinase II and of phosphorylated nucleolin which had been isolated from tumor cells grown in the presence of [32P]-o-phosphate, were identical. The partial tryptic digest revealed nine phosphopeptides. Nucleolin isolated from Krebs II mouse ascites cells was phosphorylated by purified casein kinase II with about two moles phosphate per one mole of nucleolin.

AB - Nucleolin (C23), a 110 kDa phosphoprotein, which is mainly found in the nucleolus has been shown to be a physiological substrate for casein kinase II (CKII). Nucleolin was identified and characterized by immunodetection using an anti-nucleolin antibody. Phosphopeptide patterns from nucleolin phosphorylated by purified casein kinase II and of phosphorylated nucleolin which had been isolated from tumor cells grown in the presence of [32P]-o-phosphate, were identical. The partial tryptic digest revealed nine phosphopeptides. Nucleolin isolated from Krebs II mouse ascites cells was phosphorylated by purified casein kinase II with about two moles phosphate per one mole of nucleolin.

KW - Animals

KW - Carcinoma, Ehrlich Tumor

KW - Casein Kinases

KW - Mice

KW - Nuclear Proteins

KW - Phosphoproteins

KW - Phosphorylation

KW - Protein Kinases

KW - RNA-Binding Proteins

M3 - Journal article

VL - 156

SP - 1390

EP - 1397

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -