The multiple molecular forms of glutamate dehydrogenase from pea seedlings (Pisum sativum, var. Späth's Violetta) have been investigated. When protein preparations are subjected to electrophoresis on polyacrylamide gels, the glutamate dehydrogenase can be localized by substrate staining. Shoots show seven activity bands, whereas roots have one main zone and several faint ones. SO2-fumigation generates typical alterations of the shoot zymogram. The molecular weight of all the distinct enzyme components is identical and has been shown to be 210000. Urea denaturation with subsequent renaturation of the various glutamate dehydrogenase preparations from roots, shoots and SO2-fumigated shoots results in the formation of one identical activity band on polyacrylamide gels. The results discussed here give much evidence that the multiple molecular forms of glutamate dehydrogenase from pea seedlings are conformers
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