Neurone-specific enolase and creatine phosphokinase are protein components of rat brain synaptic plasma membranes.
Neuron-specific enolase and creatine phosphokinase were found, by 2-dimensional gel analysis, in rat brain synaptic plasma membranes (SPM). The identity of these enzymes was confirmed by comigration with purified rat brain NSE and CPK and by peptide analysis. The specific enzymatic activities of enolase and creatine phosphokinase, as well as of pyruvate kinase, also present on the membranes, were comparable to those in the homogenates when these three enzymes were fully activated. In the SPM all three enzymes, particularly enolase, were partially cryptic in that enzymatic activities were very low unless the membranes were treated with Triton X-100. They were resistant to both low-salt and high-salt extraction and to trypsin, except when Triton X-100 was present. These results suggest that the enzymes are tightly bound protein components of the membrane and that they may constitute an assembly capable of generating ATP.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D003402:Creatine Kinase / Q000378:metabolism*; D009474:Neurons / Q000201:enzymology*; D017830:Octoxynol; D010751:Phosphopyruvate Hydratase / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000494:pharmacology; D011770:Pyruvate Kinase / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D013570:Synaptic Membranes / Q000201:enzymology*; D014357:Trypsin / Q000494:pharmacology
D011092:Polyethylene Glycols; D017830:Octoxynol; D011770:Pyruvate Kinase; D003402:Creatine Kinase; D014357:Trypsin; D010751:Phosphopyruvate Hydratase