Neurospora crassa glutamine synthetase. Purification by affinity chromatography and characterization of subunit structure.
Neurospora crassa glutamine synthetase was purified to homogeneity by a procedure based on affinity chromatography. The enzyme is adsorbed to a matrix of anthranilic acid bound to Sepharose and eluted with AMP. Different experimental approaches indicate that the enzyme has an octameric structure formed by subunits of identical molecular weight.
D002846:Chromatography, Affinity; D003460:Crystallization; D005974:Glutamate-Ammonia Ligase / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008970:Molecular Weight; D009491:Neurospora / Q000201:enzymology*; D009492:Neurospora crassa / Q000201:enzymology*
D046911:Macromolecular Substances; D005974:Glutamate-Ammonia Ligase