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Abstract
The variations in electrophoretic mobility of glutamine synthetase (GS) isoform Gs n1 from bean ( Phaseolus vulgaris L.) root nodules is governed by both the plant cultivar and the age of the nodule. To understand the mechanism for the variations, GS from the nodules of three cultivars and from nodules of two different ages were purified. The two subunit polypeptides (designated β and γ) of the four sources of GS were compared by two-dimensional polyacrylamide gel electrophoresis. The results revealed that the β polypeptide from all GSs had the same molecular weight and isoelectric point; similarly, the γ polypeptide from all GSs also had the same molecular weight and isoelectric point. Analysis by isoelectric focusing electrophoresis showed that the ratios of the two subunit polypeptides varied among the GSs. Furthermore, in vitro translation of isolated poly(A) + RNA also revealed changes in the ratios of the two polypeptides. These findings support the hypothesis that the variations in electrophoretic mobility are due to changes in the ratios of the two subunit polypeptides that comprised the GS.
Published Version
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