Abstract
Glutamate dehydrogenase (GDH) of Arabidopsis thaliana could be resolved by polyacrylamide gel electrophoresis into seven anodal migrating isozymes. The different isozymes behave as resulting from random association of two subunits in an hexameric complex. The number of isozymes remained unchanged in various organs of the plant, although variation was observed in the intensities of the bands. Two electrophoretic GDH variants discovered among 85 geographical races of A. thaliana were characterized by a slow (S) or normal (N) migration type. The variants have one of the two subunits in common. In heterozygotes between the two variants 22 isozymes were identified. Genetic analysis showed that the two variants N and S represent co-dominantly expressed allelic forms of the gene GDH 1.
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