THE STAINING OF LACTIC DEHYDROGENASE ISOENZYMES AFTER ELECTROPHORETIC SEPARATION ON CELLULOSE ACETATE.
Established electrophoretic techniques for the separation of the lactate dehydrogenase (L.D.H.) isoenzymes of tissues and body fluids, although of value in clinical medicine, are too elaborate for most routine laboratories. A simple method for the separation of these isoenzymes on cellulose acetate and their histochemical staining is described. Spectrophotometric estimations of the total L.D.H. activity performed on eluates of electrophoretically separated samples showed that there was no significant loss of enzyme activity during electrophoresis. The effects of alterations in pH and other practical features are discussed briefly. It is concluded that by this method isoenzymes can be studied with the same apparatus and the same routine facility as are serum proteins.
D001774:Blood Chemical Analysis; D001826:Body Fluids; D002482:Cellulose / Q000031:analogs & derivatives; D004586:Electrophoresis; D006651:Histocytochemistry; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes; D007668:Kidney; D007770:L-Lactate Dehydrogenase; D008099:Liver; D009206:Myocardium; D013194:Staining and Labeling
D007527:Isoenzymes; C005062:acetylcellulose; D002482:Cellulose; D007770:L-Lactate Dehydrogenase
BLOOD CHEMICAL ANALYSIS; BODY FLUIDS; ELECTROPHORESIS; HISTOCYTOCHEMISTRY; HYDROGEN-ION CONCENTRATION; KIDNEY; LACTATE DEHYDROGENASE; LIVER; MYOCARDIUM