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- W1423235038 abstract "This chapter discusses the assay, purification, and properties of glutamine synthetase from sheep brain. The activity of glutamine synthetase may be determined by measuring the rate of formation of inorganic phosphate, adenosine diphosphate (ADP), or glutamine. When hydroxylamine is substituted for ammonia, the product is γ-glutamylhydroxamate, which gives a characteristic brown color on the addition of ferric chloride. The enzyme also catalyzes a γ-glutamyl transfer reaction, which requires catalytic quantities of nucleotide (adenosine triphosphate (ATP) or ADP) and also inorganic phosphate (or arsenate, Asi). The transfer reaction may also be followed by use of the ferric chloride reagent. The native enzyme can be dissociated by several procedures to a monomer of molecular weight about 60,000. Ultracentrifugal studies and electron microscopy shows that the enzyme consists of eight apparently identical subunits. The enzyme is homogeneous on electrophoresis on acrylamide gel and on free electrophoresis. The isoelectric point of the enzyme determined from free electrophoresis studies is 4.2. The enzyme is protected against heat inactivation at 60° by ATP (or ADP) and magnesium." @default.
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- W1423235038 date "1970-01-01" @default.
- W1423235038 modified "2023-10-06" @default.
- W1423235038 title "[129] Glutamine synthetase (sheep brain)" @default.
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- W1423235038 doi "https://doi.org/10.1016/0076-6879(71)17304-1" @default.
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