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G2751

Sigma-Aldrich

Glutamic-Oxalacetic Transaminase from porcine heart

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

Sinonimo/i:

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

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About This Item

Numero CAS:
Classificazione EC (Enzyme Commission):
Numero CE:
Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.54

Tipo

Type I

Forma fisica

ammonium sulfate suspension

Attività specifica

200-500 units/mg protein

Attività estranea

glutamic-pyruvic transaminase ≤0.03%
lactic dehydrogenase ≤0.01%
malic dehydrogenase ≤0.01%

Condizioni di spedizione

wet ice

Temperatura di conservazione

2-8°C

Descrizione generale

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.

Applicazioni

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

Azioni biochim/fisiol

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.

Definizione di unità

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.

Stato fisico

Suspension in 3.0 M (NH4)2SO4 containing 0.05 M maleate and 2.5 mM α-ketoglutarate, pH 6.0

Risultati analitici

Protein determined by biuret.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)


Certificati d'analisi (COA)

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Biochimica et biophysica acta, 1857(9), 1561-1568 (2016-06-12)
Mitochondrial Complex II is a key mitochondrial enzyme connecting the tricarboxylic acid (TCA) cycle and the electron transport chain. Studies of complex II are clinically important since new roles for this enzyme have recently emerged in cell signalling, cancer biology
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The laboratory rabbit, guinea pig, hamster, and other rodents., 57-116 (2012)
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)
Pyridoxal 5-phosphate-dependent enzymes: catalysis, conformation, and genomics
Comprehensive Natural Products II (2010)
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

Articoli

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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