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J. Biol. Chem., Vol. 255, Issue 6, 2231-2234, Mar, 1980

Heterogeneity of glutamine synthetase polypeptides in Neurospora crassa

F Sanchez, E Calva, M Campomanes, L Blanco, J Guzman, JL Saborio and R Palacios

Purified preparations of Neurospora crassa glutamine synthetase contain two nonidentical polypeptides that can be separated by acrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and 7 M urea. These polypeptides are synthesized both in vivo and in a heterologous cell-free protein-synthesizing system. The data presented indicate that both polypeptides contain an active site for glutamine synthetase activity and suggest that there is not a precursor-product relationship between them.
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