title: Heterogeneity of glutamine synthetase polypeptides in Neurospora crassa.
abstract: 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.
mesh_terms: D005974:Glutamate-Ammonia Ligase / Q000378:metabolism*; D046911:Macromolecular Substances; D008970:Molecular Weight; D009491:Neurospora / Q000201:enzymology*; D009492:Neurospora crassa / Q000201:enzymology*; D010455:Peptides / Q000032:analysis
chemical_list: D046911:Macromolecular Substances; D010455:Peptides; D005974:Glutamate-Ammonia Ligase