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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-571-9
MDL number:
Specific activity:
200-500 units/mg protein
type
Type I
Quality Level
form
ammonium sulfate suspension
specific activity
200-500 units/mg protein
foreign activity
glutamic-pyruvic transaminase ≤0.03%, lactic dehydrogenase ≤0.01%, malic dehydrogenase ≤0.01%
shipped in
wet ice
storage temp.
2-8°C
General description
Research area: Cellsignaling. Glutamic-Oxalacetic Transaminase is found in all tissues and is predominant in the liver and skeletal muscle. It is a prototype of fold-type I pyridoxal 5′-phosphate (PLP)-enzymes. Glutamic-oxalacetic transaminase is a homodimer containing large and small domains in each subunit.
Application
Glutamic-OxalaceticTransaminase from porcine heart is suitable for the preparation ofphenylalanine amino acid. The immobilized form of this enzyme maybe used incomparison studies between soluble and immobilized forms in terms of reactionefficiency and stability.
Glutamic-Oxalacetic Transaminase from porcine heart has been used:
- in an enzyme-coupled assay for evaluating L-asparaginase enzyme activity
- in microtiter plate format enzyme-based assay to estimate malic acid content in berry samples
- as a supplement in homogenization buffers for the isolation of heart mitochondrial membranes in the presence of oxaloacetate (OAA)-depleting system
Biochem/physiol Actions
Glutamic-oxalacetic transaminase or aspartate aminotransferase (AAT) catalyzes the interconversion of L-aspartate and α-ketoglutarate with oxalacetate and L-glutamate. This reversible transaminase reaction is dependent on pyridoxal 5′-phosphate (PLP). Glutamic-oxalacetic transaminase maintains the nitrogen currency for metabolism by generating L-glutamate. Elevated serum levels of glutamic-oxalacetic transaminase are indicated in myocardial infarction, liver diseases, and some renal diseases.
Physical form
Suspension in 3.0 M (NH4)2SO4 containing 0.05 M maleate and 2.5 mM α-ketoglutarate, pH 6.0
Analysis Note
Protein determined by biuret.
Other Notes
One unit will convert 1.0 μmole of α-ketoglutarate to L-glutamate per min at pH 7.5 at 37 °C, in the presence of L-aspartic acid. One unit is equivalent to ~2,000O.D. (Karmen) units at 25 °C.
Storage Class
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - Skin Sens. 1
Regulatory Information
低风险生物材料
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Articles
以硫酸铵悬浮液形式提供的酶的使用指南
Instructions for working with enzymes supplied as ammonium sulfate suspensions
Related Content
The Study of Serum GOT (Glutamic Oxalacetic Transaminase) Activity and Some kinetic Parameters in Patient with Pulmonary Tuberculosis
Ismahil PA and Hassan LM
Biological Chemistry, 23, 159-169 (2017)
Michael D Toney
Archives of biochemistry and biophysics, 544, 119-127 (2013-10-15)
Aspartate aminotransferase (AAT) is a prototypical pyridoxal 5'-phosphate (PLP) dependent enzyme that catalyzes the reversible interconversion of l-aspartate and α-ketoglutarate with oxalacetate and l-glutamate via a ping-pong catalytic cycle in which the pyridoxamine 5'-phosphate enzyme form is an intermediate. There
C Mavrides et al.
The Journal of biological chemistry, 250(11), 4128-4133 (1975-06-10)
Two aminotransferases from Escherichia coli were purified to homogeneity by the criterion of gel electrophoresis. The first (enzyme A) is active on L-aspartic acid, L-tyrosine, L-phenylalanine, and L-tryptophan; the second (enzyme B) is active on the aromatic amiono acids. Enzyme
Global Trade Item Number
| SKU | GTIN |
|---|---|
| G2751-2KU | 04061832924014 |
| G2751-10KU | 04061832923994 |
| G2751-1KU | 04061833629369 |
