Inhibition of lactate dehydrogenase isoenzymes by sodium perchlorate evaluated.
We evaluated a method of measuring lactate dehydrogenase isoenzyme 1 (LD-1) selectively (Clin Chem 1987;33:991-2), in which all other LD isoenzymes were inhibited by adding sodium perchlorate to the reaction medium to a final concentration of 0.825 mol/L. In this study we used the different isoenzymes purified from human autopsy tissue and found that the originally published amount of inhibitor (a) increased the original LD-1 activity and (b) did not eliminate all enzyme activity of LD-2 and LD-3. Interference by LD-2 was further demonstrated. Thus we conclude that this method cannot be used for the selective determination of LD-1 because its results do not accurately reflect the original LD-1 activity.
Sanders
G T
GT
Department of Clinical Chemistry, Academic Medical Center, Amsterdam, The Netherlands.
van der Neut
E
E
van Straalen
J P
JP
D006801:Humans; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors* / Q000302:isolation & purification; D010472:Perchlorates / Q000494:pharmacology*; D017670:Sodium Compounds
D007527:Isoenzymes; D010472:Perchlorates; D017670:Sodium Compounds; C031068:sodium perchlorate; D007770:L-Lactate Dehydrogenase