Chloroform markedly stimulates the phosphorylation of myelin basic proteins.
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).
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000378:metabolism; D002725:Chloroform / Q000494:pharmacology*; D007700:Kinetics; D051379:Mice; D004676:Myelin Basic Protein / Q000378:metabolism*; D009186:Myelin Sheath / Q000378:metabolism; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation
D004676:Myelin Basic Protein; D010761:Phosphorus Radioisotopes; D002725:Chloroform; D000255:Adenosine Triphosphate