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RESEARCH PRODUCT
The Influence of Thiol Reagents on the Isoenzyme Pattern of Plant L+Lactate Dehydrogenase (EC 1.1.1.27)
Alfred CörperGunter M. Rothesubject
Thiol Reagentsfood and beveragesGeneral MedicineGlutathioneIsozymeMolecular biologyIsoenzyme patternElectrophoresischemistry.chemical_compoundchemistryBiochemistryLactate dehydrogenaseCysteamineCysteinedescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1978-08-01 | Zeitschrift für Pflanzenphysiologie |