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Plant Physiology 77:791-794 (1985)
© 1985 American Society of Plant Biologists

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Characterization of Glutamine Synthetase Isoforms from Chlorella1

Rob F. Beudeker2 and F. Robert Tabita

Center for Applied Microbiology, The University of Texas at Austin, Austin, Texas 78712-1095, Department of Microbiology, The University of Texas at Austin, Austin, Texas 78712-1095

Ion-exchange chromatography of extracts derived from Chlorella sorokiniana mutant strain (oxygen resistant) yielded two separate activity peaks of glutamine synthetase (GS). GSI and GSII were purified 220- and 187-fold and have molecular weights of approximately 398,000 and 360,000, respectively. Both enzymes are composed of eight identical subunits with a subunit molecular weight of 47,000 for GSI and 43,000 for GSII. The amino acid composition, catalytic, and immunological properties for both enzymes are similar.


2 Present Address: R. F. Beudeker, Gist-Brocades, Section FOG, 2600 MA Delft, The Netherlands.

1 Supported in part by Dow Chemical Company.




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Mol Biol EvolHome page
D. L. Robertson and A. Tartar
Evolution of Glutamine Synthetase in Heterokonts: Evidence for Endosymbiotic Gene Transfer and the Early Evolution of Photosynthesis
Mol. Biol. Evol., May 1, 2006; 23(5): 1048 - 1055.
[Abstract] [Full Text] [PDF]




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Copyright © 1985 by the American Society of Plant Biologists