[Purification, properties and quaternary structure of glutamine synthetase from Chlorella].
A highly purified preparation of glutamine synthetase from chlorella grown on a medium containing nitrate as a sole source of nitrogen, was isolated and characterized by disc-electrophoresis and analytical ultracentrifugation. The N-terminal amino acid of glutamine synthetase is glycine. The molecular weight of glutamine synthetase is 32.000; its activity in the presence of Mg2+ was 150 mkmol o-phosphate per min per mg protein. The molecular weight of subunits of the enzyme, equal to 53.000 was determined by disc-electrophoresis in polyacrylamide gel in the presence of sodium dodecyl sulfate. Electron microscopy of negatively contrasted enzyme preparations revealed 6 subunits in the enzyme molecule, arranged in a point symmetry group 32.
D002708:Chlorella / Q000201:enzymology*; D003470:Culture Media; D005974:Glutamate-Ammonia Ligase / Q000302:isolation & purification* / Q000378:metabolism; D046911:Macromolecular Substances; D008274:Magnesium / Q000494:pharmacology; D008970:Molecular Weight
D003470:Culture Media; D046911:Macromolecular Substances; D005974:Glutamate-Ammonia Ligase; D008274:Magnesium
Ochistka, svoĭstva i chetvertichnaia struktura glutaminsintetazy Khlorelly