A kinetic method for quantification of aspartate aminotransferase isoenzymes.
A spectrophotometric assay is proposed to determine the levels of aspartate aminotransferase (AAT) isoenzymes from chicken liver by a steady-state kinetic method which depends on the differential inhibition of these isoenzyme forms by high concentrations of substrate 2-oxoglutarate at pH 6.2. The use of a standard curve permits the determination of the percentage of chicken liver c-AAT and m-AAT isoenzymes. This method yields results in good correlation with those achieved by different extent adipate inhibition and by differential centrifugation.
Departament de Bioquímica i Fisiologia, Facultat de Química, Universitat de Barcelona, Spain.
R
R
Gracia
M
M
Busquets
M
M
Gil
A
A
Cortés
J
J
Bozal
D000818:Animals; D001219:Aspartate Aminotransferases / Q000032:analysis*; D002645:Chickens; D003600:Cytosol / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000032:analysis*; D007656:Ketoglutaric Acids / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008930:Mitochondria, Liver / Q000201:enzymology
D007527:Isoenzymes; D007656:Ketoglutaric Acids; D001219:Aspartate Aminotransferases