form
lyophilized powder
specific activity
100-400 units/mg protein
composition
Protein, ≥30% biuret
solubility
H2O: soluble 0.95-1.05 mg/mL, clear to slightly hazy
UniProt accession no.
storage temp.
−20°C
Gene Information
Escherichia coli K12 ... glnA(948370)
Application
L-谷氨酰胺合成酶可用于从大肠杆菌中纯化蛋白酶。
Biochem/physiol Actions
谷氨酸降解酶
L-谷氨酰胺合成酶催化L-谷氨酸和氨缩合为L-谷氨酰胺。它是谷氨酸的降解酶。
Physical form
含缓冲盐和稳定剂的冻干粉
Preparation Note
在含葡萄糖和 NH4Cl 的培养基中生长
Other Notes
一个单位将在37℃,pH值7.1下于15分钟内将1.0μ摩尔的L-谷氨酸转化为L-谷氨酰胺。
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
此项目有
H S Kingdon et al.
Journal of bacteriology, 94(4), 949-957 (1967-10-01)
The kinetic properties of Escherichia coli glutamine synthetase are markedly influenced by the manner in which the organism is grown. Enzyme obtained from stationary-phase cells grown on glycerol and glutamate is strongely inhibited by each of the eight feedback effectors
E Rodriguez et al.
Plant physiology and biochemistry : PPB, 62, 19-22 (2012-11-24)
Lead (Pb) is a toxic element, but its putative mutagenic effects in plant cells, using molecular markers, remain to unveil. To evaluate if Pb induces mutagenicity, Pisum sativum L. seedlings were exposed to Pb(2+) (up to 2000 mg L(-1)) for 28 days
S H Liaw et al.
Protein science : a publication of the Protein Society, 4(11), 2358-2365 (1995-11-01)
Glutamine synthetase (GS) catalyzes the ATP-dependent condensation of ammonia and glutamate to yield glutamine, ADP, and inorganic phosphate in the presence of divalent cations. Bacterial GS is an enzyme of 12 identical subunits, arranged in two rings of 6, with
Beatriz Sánchez-Pardo et al.
Journal of plant physiology, 170(3), 265-271 (2012-12-19)
The aims of this work were to investigate the microlocalisation of cadmium (Cd) in Lupinus albus L. cv. Multolupa nodules, and to determine its effects on carbon and nitrogen metabolism. Nodulated white lupin plants were grown in a growth chamber
Purification of a protease from Escherichia coli with specificity for oxidized glutamine synthetase.
J E Roseman et al.
The Journal of biological chemistry, 262(5), 2101-2110 (1987-02-15)
A soluble Escherichia coli protease has been identified and purified to homogeneity. The protease cleaves glutamine synthetase which has been modified by mixed function oxidation; native glutamine synthetase is not a substrate. Using [14C]glutamine synthetase as a substrate (prepared by
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