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Cereal Chem 43:517 - 528.  |  VIEW ARTICLE

The Oxidation-Reduction Enzymes of Wheat. I. A Qualitative Investigation of the Dehydrogenases.

G. R. Honold, G. L. Farkas, and M. A. Stahmann. Copyright 1966 by the American Association of Cereal Chemists, Inc. 

A qualitative investigation of dehydrogenases in whole wheat and five milling fractions of two hard red winter (Triumph and Bison) and spring (Lee and Selkirk) wheats was made. Homogenates were prepared in aqueous sucrose and assayed by polyacrylamide gel electrophoresis, followed by incubation of the gels in substrate solutions and coupling of the enzymatic reaction with reduction of nitro-blue tetrazolium. Isoenzyme bands were detected for the dehydrogenases of glucose-6-phosphate, 6-phosphogluconate, malate, isocitrate, alpha-ketoglutarate, succinate, glutamate, alcohol, and lactate. Significant activities were seen in flour, particularly of the spring wheats. The number of observed isoenzyme bands varied from one for lactate, alpha-ketoglutarate, and isocitrate dehydrogenases to eleven for malate dehydrogenase. The number of isoenzyme bands and level of dehydrogenase activity were generally higher in the two spring wheats than in the two winter wheats.

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