0000000000671314
AUTHOR
Alfred Cörper
Affinity chromatographic separation of plant lactate dehydrogenase
Abstract Lactate dehydrogenase from potato tubers was purified by the use of several standard purification procedures as well as by affinity chromatography on C
The Influence of Thiol Reagents on the Isoenzyme Pattern of Plant L+Lactate Dehydrogenase (EC 1.1.1.27)
Summary Lactate dehydrogenase from potato tubers was incubated together with various thiol reagents and the effect on the electrophoretic behavior of its isoenzymes studied. while disulfides, alkylating agents, and H202 did not alter the number and electrophoretic behavior of the isoenzymes of L + LDH, reduced glutathione and 2-mercaptoethanol led to an increase in the number of isoenzymes. The reaction was dependent on concentration and pH. On the other hand, cysteine and cysteamine had no such effect. Results are discussed in view of the possible secondary nature of the plant LDH isoenzymes.