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Chloroform markedly stimulates the phosphorylation of myelin basic proteins.

Abstract
We have investigated the effect of chloroform on the phosphorylation of myelin basic proteins because tumor-promoting agents such as phorbol esters and chloroform are known to enhance the activity of protein kinase C. We report that the presence of chloroform, at a concentration known to enhance protein kinase C activity, stimulated the phosphorylation of myelin basic proteins 15-17 fold over control conditions. The phosphorylation of a 50 kiloDalton myelin protein was also stimulated but to a lesser extent. The concentration of chloroform required for the maximal phosphorylation of myelin basic proteins and the 50 kiloDalton protein was approximately 2% (v/v).
AuthorsJ B Ulmer, P E Braun
JournalBiochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 146 Issue 3 Pg. 1084-8 (Aug 14 1987) ISSN: 0006-291X [Print] United States
PMID2441700 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Myelin Basic Protein
  • Phosphorus Radioisotopes
  • Chloroform
  • Adenosine Triphosphate
Topics
  • Adenosine Triphosphate (metabolism)
  • Animals
  • Brain (metabolism)
  • Chloroform (pharmacology)
  • Kinetics
  • Mice
  • Myelin Basic Protein (metabolism)
  • Myelin Sheath (metabolism)
  • Phosphorus Radioisotopes
  • Phosphorylation

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