Cereal Chem 44:373 - 382.  |  VIEW ARTICLE
The Oxidation-Reduction Enzymes of Wheat. II. A Quantitative Investigation of the Dehydrogenases.

G. R. Honold, G. L. Farkas, and M. A. Stahmann. Copyright 1967 by the American Association of Cereal Chemists, Inc. 

Two hard red winter wheats, Triumph and Bison, and two hard red spring wheats, Lee and Selkirk, along with five milling fractions of each, were quantitatively assayed for dehydrogenases of glucose-6-phosphate, 6-phosphogluconate, malate, isocitrate, succinate, glutamate, lactate, and alcohol. Crude enzyme extracts were prepared in aqueous sucrose. Assays were conducted by conventional spectrophotometric methods and by densitometric tracings of reduced nitro-blue tetrazolium on polyacrylamide gels. Malate dehydrogenase showed no significant variation between winter and spring wheat and was 100 to 1,000 times more active than any other dehydrogenase studied. Glucose-6-phosphate, 6-phosphogluconate, isocitrate, and alcohol dehydrogenases were detected in significant amounts. Low levels of activity were detected for dehydrogenases of lactate, succinate, and glutamate. Generally, the spring wheats contained significantly higher dehydrogenase activity. High levels of activity were detected for many dehydrogenases in flour, particularly from spring wheat. Lee wheat contained more dehydrogenase activity than any of the other varieties.