Isolation and purification of creatine kinase conversion factor from human serum and its identification as carboxypeptidase N.
Creatine kinase conversion factor has been isolated from human serum and purified to electrophoretic and chromatographic homogeneity. The enzyme sequentially converts creatine kinase MM3 to MM2 and MM1 and hydrolyzes lysine and arginine from hippuryl-L-lysine and hippuryl-L-arginine. Data on molecular weight, (316,000 dalton), electrophoretic mobility (alpha-globulin), prevalence in serum (26 mg/L), subunit composition (two subunits, 80,000 and 52,200 dalton) indicate that creatine kinase conversion factor is identical to carboxypeptidase N. The previously reported lower molecular weight of 190,000 dalton of partially purified creatine kinase conversion factor is attributed to proteolytic degradation.
D002268:Carboxypeptidases / Q000302:isolation & purification*; D002850:Chromatography, Gel; D003402:Creatine Kinase / Q000378:metabolism; D004587:Electrophoresis, Agar Gel; D006801:Humans; D007527:Isoenzymes; D008239:Lysine / Q000031:analogs & derivatives / Q000378:metabolism; D001121:Lysine Carboxypeptidase / Q000097:blood / Q000302:isolation & purification*; D008970:Molecular Weight
D007527:Isoenzymes; C007945:hippuryl-L-lysine; D003402:Creatine Kinase; D002268:Carboxypeptidases; C042458:carboxypeptidase K; D001121:Lysine Carboxypeptidase; D008239:Lysine