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G2751

Sigma-Aldrich

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:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type I

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.

Unit Definition

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.

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
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

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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