Studies on Cenditions for Measurement of Human LD Activity
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Optimum reaction conditions at 37° for spectrophotometric assay of activity (from lactate to pyruvate) of human LDH isoenzymes were determined with respect to buffer concentration, NAD concentration, substrate concentration and pH.<BR>Human LDH isoenzymes used were separated by column chromatography.<BR>Optimum concentration of Glycine-NaOH buffer were within the range of 0.1M to 0.2M for LDH<SUB>1</SUB> and LDH<SUB>5</SUB> isoenzymes. An optimum activity was obtained at a NAD concentration of 4.5×10<SUP>-3</SUP>M. optimum concentration of DL-lactate was 0.25M for total LDH, since it was 0.1M for LDH<SUB>1</SUB>and0.5M for LDH<SUB>5</SUB>.<BR>Activities of LDH<SUB>1</SUB>and LDH<SUB>5</SUB>were enhanced with the increase of pH, when the activities were compared between of 9.0-10.8.<BR>Although Fendley reported that the LDH5 isoenzyme was unable to measure when the assay was performed of pH 10.0, we have found that the LDH<SUB>5</SUB> isoenzyme activity can measure when a LDH·NAD complex is formed by a preincubation for 5min. and the reaction is started by a substrate buffer.
- Japan Society of Clinical Chemistryの論文
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