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Merck

T0581

Sigma-Aldrich

转谷氨酰胺酶 来源于天竺鼠

≥1.5 units/mg protein, recombinant, expressed in E. coli

别名:

TGase

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About This Item

分類程式碼代碼:
12352204
NACRES:
NA.54

重組細胞

expressed in E. coli

品質等級

比活性

≥1.5 units/mg protein

運輸包裝

dry ice

儲存溫度

−20°C

應用

10 mM氯化钙用于激活酶。
转谷氨酰胺酶已用于一项可改善可量化分析研究,以充分表征转谷氨酰胺酶在亨廷顿氏病和阿尔茨海默病等疾病中的作用。转谷氨酰胺酶还用于研究转谷氨酰胺酶活性的非放射性斑点印迹试验。

單位定義

一个单元,在pH6.0,37℃下,每分钟将催化Nα-Z-Gln-Gly和羟胺形成1.0 μ摩尔的异羟肟酸酯。(L-谷氨酸γ-单羟肟酸酯为参考标准。)

外觀

从50 mM NaH2PO4、150 mM NaCl、pH 8冻干。包含麦芽糖糊精。

象形圖

Exclamation mark

訊號詞

Warning

危險聲明

危險分類

Eye Irrit. 2

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Acyl-CoA esters of xenobiotic carboxylic acids as biochemically active intermediates.
H S Sherratt
Biochemical Society transactions, 13(5), 856-858 (1985-10-01)
K D MacDermot et al.
Developmental pharmacology and therapeutics, 3(3), 150-159 (1981-01-01)
We report investigations of benzoate and glycine metabolism and glycine acyltransferase activity in rats. These studies provide insights related to the therapy and pathophysiology of human nonketotic hyperglycinemia. Liver acyltransferase activity increased sharply postnatally from low levels at birth, but
S Kølvraa et al.
Biochemical medicine and metabolic biology, 36(1), 98-105 (1986-08-01)
Prompted by the fact that the urinary excretion of organic acids in the riboflavin-deficient rat closely mimics that found in patients with inborn errors in the acyl-CoA dehydrogenation systems, the organelle localization and the apparent kinetic constants (Km and Vmax
M Kelley et al.
Journal of biochemical toxicology, 5(2), 125-135 (1990-01-01)
The aralkyl-CoA:glycine N-acyltransferase and the arylacetyl-CoA:amino acid of N-acyltransferase were purified from bovine liver mitochondria and their response to a variety of ions investigated. The activity of the aralkyl transferase was inhibited by divalent cations with all substrates investigated. For
M Kelley et al.
Biochemical pharmacology, 35(2), 289-295 (1986-01-15)
The amino acid conjugation of the phenoxyherbicides 2,4-dichlorophenoxyacetate (2,4-D) and 2,4,5-trichlorophenoxyacetate (2,4,5-T) by animals was examined at the level of the enzymes catalyzing the reactions. The phenoxyherbicides were not substrates for the bile acid conjugating system but were substrates for

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