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Effects of Protein Phosphorylation on the Sulphonylurea Receptor of the Pancreatic β-Cell

  • Ichiro Niki
  • Barbara Coles
  • Frances M. Ashcroft
  • Stephen J. H. Ashcroft
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 426)

Abstract

There is evidence that protein phosphorylation may modulate the action of diazoxide on the β-cell K-ATP channel [1] and the sulphonylurea receptor [2–3]. In this paper, we have further investigated the role of phosphorylation in the action of diazoxide on the β-cell sulphonylurea receptor by carrying out time-course studies on inhibition of [3H]-gliben-clamide binding by MgATP and diazoxide, and by examining effects of phosphatase inhibitors on binding. We also investigated the presence of protein kinase and protein phosphatase activities in β-cell membrane fractions.

Keywords

Protein Phosphorylation Okadaic Acid Photoaffinity Label United Kingdom Introduction Sulphonylurea Receptor 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Ichiro Niki
    • 1
  • Barbara Coles
    • 1
  • Frances M. Ashcroft
    • 1
  • Stephen J. H. Ashcroft
    • 1
  1. 1.Nuffield Department of Clinical BiochemistryJohn Radcliffe Hospital HeadingtonUK

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