Isolation of human lactate dehydrogenase isoenzyme X by affinity chromatography.
Human isoenzyme LDH-X (lactate dehydrogenase isoenzyme X) was isolated from seminal fluid of frozen semen samples by affinity chromatography by using oxamate-Sepharose and AMP-Sepharose. In the presence of 1.6 mM-NAD+, isoenzyme LDH-X does not bind to AMP-Sepharose, whereas the other lactate dehydrogenase isoenzymes do. This is the crucial point in the isolation of isoenzyme LDH-X from the other isoenzymes. The purified human isoenzyme LDH-X had a specific activity of 146 units/mg of protein.
D000249:Adenosine Monophosphate; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000302:isolation & purification*; D009243:NAD; D010072:Oxamic Acid; D012685:Sepharose
D007527:Isoenzymes; D009243:NAD; D000249:Adenosine Monophosphate; D012685:Sepharose; D007770:L-Lactate Dehydrogenase; D010072:Oxamic Acid