A comparison of potato and vertebrate lactate dehydrogenases.
A 2000-fold purification of L(+)-lactate dehydrogenase from potatoes is reported. Five isoenzymes of lactate dehydrogenase can be detected in crude extracts of potato, and three of these are present in the purified preparation. The enzyme (mol.wt. 150 000), which is composed of four subunits (mol.wt. 37 500), is active with the same oxo acids and hydroxy acids that have been reported as substrates with the same oxo acids and hydroxy acids that have been reported as substrates for vertebrate lactate dehydrogenases. These similarities between potato and vertebrate lactate dehydrogenases contrast sharply with some other reports on potato lactate dehydrogenase. These discrepancies are discussed in relation to the proposition that vertebrate and potato lactate dehydrogenases share a common evolutionary origin.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D055598:Chemical Phenomena; D002621:Chemistry; D007527:Isoenzymes; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D010070:Oxalates / Q000494:pharmacology; D010072:Oxamic Acid / Q000494:pharmacology; D010944:Plants / Q000201:enzymology*; D013379:Substrate Specificity
D007527:Isoenzymes; D010070:Oxalates; D000255:Adenosine Triphosphate; D007770:L-Lactate Dehydrogenase; D010072:Oxamic Acid