Chemical phosphorylation of proteins by zinc-ATP

  • Jarvis B
  • Chinander L
  • Wettlaufer J
 et al. 
  • 3

    Readers

    Mendeley users who have this article in their library.
  • 7

    Citations

    Citations of this article.

Abstract

During an examination of in vitro phosphorylation of the adipocyte lipid-binding protein (ALBP) by the insulin receptor, we detected insulin receptor-independent, chemical phosphorylation of ALBP. This activity was present in ALBP purified to homogeneity from murine 3T3-L1 cells and in recombinant murine ALBP purified from expressing E. coli cultures. Phosphoamino acid analysis revealed that chemical phosphorylation of ALBP occurred primarily on Ser residues. The phosphorylation activity occurred in the alkaline pH range from 8 to 11 and exhibited a broad temperature dependence. The reaction rate was linearly dependent upon the ATP concentration and exhibited a biphasic kinetic profile. Eight of twelve other proteins tested also underwent chemical phosphorylation. Zn+2, Mg+2, or Mn+2promoted optimal phosphorylation of different proteins. We conclude that many proteins are capable of undergoing chemical phosphorylation. © 1989.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

  • Bruce W. Jarvis

  • Laurie L. Chinander

  • Jacque R. Wettlaufer

  • David A. Bernlohr

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free