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G2751

Sigma-Aldrich

Glutamic-Oxalacetic Transaminase from porcine heart

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

Synonyme(s) :

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

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About This Item

Numéro CAS:
9000-97-9
Numéro de classification (Commission des enzymes):
2.6.1.1 (BRENDA, IUBMB)
Numéro CE :
232-571-9
Numéro MDL:
MFCD00131191
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Type

Type I

Forme

ammonium sulfate suspension

Activité spécifique

200-500 units/mg protein

Activité étrangère

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

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Description générale

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

Actions biochimiques/physiologiques

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.

Définition de l'unité

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.

Forme physique

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

Remarque sur l'analyse

Protein determined by biuret.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Anna Stepanova et al.
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
Clinical biochemistry and hematology
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
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