Creatine kinase activity in the Torpedo electrocyte and in the nonreceptor, peripheral v proteins from acetylcholine receptor-rich membranes.
The nonreceptor, peripheral v proteins (Mr 43,000 proteins) are conspicuous components of the acetylcholine receptor-rich membranes and the Torpedo electrocyte, so far devoid of any known enzymatic function. Creatine kinase (adenosine 5'-triphosphate:creatine N-phosphotransferase, EC 2.7.3.2) is identified in distinct polypeptides belonging to the family of v proteins. Embryonic (70- to 90-mm embryos), neonatal, and adult electric organs of Torpedo marmorata contain two isoenzymes of creatine kinase: the BB (brain) and the MM (muscle) forms. The proportion of the two isoenzymes does not appear to change in the course of ontogenic and postnatal development. Only the BB isoenzyme appears to be associated with the acetylcholine-rich membranes in adult Torpedo. The creatine kinase can be purified to homogeneity by chromatographic procedures that exploit the richness in free sulfhydryl groups of the enzyme. Specific activities of 150 units/mg are obtained from electric tissue. The enzyme subunits identified by two-dimensional gel electrophoresis and immunoblotting techniques have pI values in the 6.0-6.5 region and apparent molecular weights in the 40,000-43,000 range, the latter values depending on redox conditions.
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D003402:Creatine Kinase / Q000302:isolation & purification / Q000378:metabolism*; D004557:Electric Organ / Q000201:enzymology* / Q000254:growth & development; D004591:Electrophoresis, Polyacrylamide Gel; D004625:Embryo, Nonmammalian; D008565:Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism*; D011950:Receptors, Cholinergic / Q000302:isolation & purification / Q000378:metabolism*; D014101:Torpedo
D008565:Membrane Proteins; D011950:Receptors, Cholinergic; D003402:Creatine Kinase