Physicochemical and catalytic properties of aspartate aminotransferase selectively modified at the tyrosine and cysteine residues.
D000818:Animals; D001059:Apoproteins / Q000378:metabolism; D001219:Aspartate Aminotransferases / Q000378:metabolism*; D001665:Binding Sites; D002250:Carbon Radioisotopes; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D002942:Circular Dichroism; D003545:Cysteine; D004590:Electrophoresis, Paper; D004789:Enzyme Activation; D005033:Ethylmaleimide; D007655:Ketoglutarate Dehydrogenase Complex; D008697:Methane; D009206:Myocardium / Q000201:enzymology; D009574:Nitro Compounds; D011485:Protein Binding; D011487:Protein Conformation; D011732:Pyridoxal Phosphate; D013053:Spectrophotometry; D013056:Spectrophotometry, Ultraviolet; D013438:Sulfhydryl Compounds; D014443:Tyrosine / Q000032:analysis
D001059:Apoproteins; D002250:Carbon Radioisotopes; D009574:Nitro Compounds; D013438:Sulfhydryl Compounds; D014443:Tyrosine; D011732:Pyridoxal Phosphate; D007655:Ketoglutarate Dehydrogenase Complex; D001219:Aspartate Aminotransferases; D003545:Cysteine; D005033:Ethylmaleimide; D008697:Methane