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Aspartate amino transferase iso enzymes in the poly ploid wheats and their di ploid relatives on the origin of tetra ploid wheats



Aspartate amino transferase iso enzymes in the poly ploid wheats and their di ploid relatives on the origin of tetra ploid wheats



Biochemie und Physiologie der Pflanzen (BPP) 170(2): 159-171



Polyacrylamide gel electrophoresis resolves 3 major and 2 minor aspartate aminotransferase isoenzymes from seedling extracts of wheats and diploid goatgrasses. The 3 major isoenzymes designated AAT-A, AAT-B and AAT-C (in order of their decreasing anodal electrophoretic mobility) are genetically controlled by 3 separate gene loci and differ in their intracellular localization and solubility properties. A different extent of interspecific, intraspecific or intrapopulational variation in all 3 AAT isoenzymes was observed among diploid goatgrasses, while in wheats the variation was mostly correlated with the ploidy level. The origin of tetraploid wheats has resulted in fixation of heterozygosity at the AAT-C locus and the origin of the hexaploid Triticum aestivum L. in an additional fixation of heterozygosity at the AAT-B locus. Dimeric quaternary structure of the 2 isoenzymes, AAT-B and AAT-C, can be assumed from the appearance of triplet electrophoretic phenotypes with a hybrid heterodimer and 2 parental homodimers in polyploid wheats and in heterozygous individuals of some goatgrasses. Among the contemporary diploid goatgrasses, only Aegilops speltoides Tausch proved suitable for the role of the wheat B-genome donor with respect to AAT-B and AAT-C electrophoretic variants.

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