PMID: 25837Apr 1, 1978

Purification and characterization of aromatic-amino-acid-glyoxylate aminotransferase from monkey and rat liver

Hoppe-Seyler's Zeitschrift für physiologische Chemie
I HaradaR Kido


Aromatic-amino-acid-glyoxylate aminotransferase was highly purified from the mitochondrial fraction of livers from monkey and glucagon-injected rats. The two enzyme preparations showed physical and enzymic properties different from a kynurenine aminotransferase previously described. The two enzymes had nearly identical molecular weights (approximate 80 000), isoelectric points (pH 8.0) and pH optima (pH 8.0 - 8.5). However, a difference in substrate specificity was observed between the two enzymes. Both enzymes utilized glyoxylate, pyruvate, hydroxypyruvate and 2-oxo-4-methyl-thiobutyrate as effective amino acceptors. 2-Oxoglutarate was active for rat enzyme but not for monkey enzyme. With glyoxylate, amino donors were effective in the following order of activity; phenylalanine greater than histidine greater than tyrosine greater than tryptophan greater than 5-hydroxytrypotphan greater than kynurenine for the rat enzyme, and phenylalanine greater than kynurenine greater than histidine greater than tryptophan greater than 5-hydroxy-tryptophan for the monkey enzyme.


Mar 1, 1991·Brain Research·E OkunoR Schwarcz
Feb 4, 1999·Journal of Neurochemistry·P S HodgkinsR Schwarcz
May 28, 2013·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Guoxiang XieWei Jia

Related Concepts

Glucagon (rDNA)
Enzymes, antithrombotic
Alpha Ketoglutarate
Pyruvate Measurement
Mitochondria, Liver

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