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G2751

Glutamic-Oxalacetic Transaminase from porcine heart

Type I, ammonium sulfate suspension, 200-500 units/mg protein

Synonym(s):

L-Aspartate:2-oxoglutarate aminotransferase, Aspartate Aminotransferase, GOT

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About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-571-9
MDL number:
EC Number:
Specific activity:
200-500 units/mg protein
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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)

pictograms

Exclamation mark

signalword

Warning

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


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

SKUGTIN
G2751-2KU04061832924014
G2751-10KU04061832923994
G2751-1KU04061833629369