アミノ酸酸化アポ酵素と人腎臓に就いて

Abstract

As the prosthetic group of aminoacidoxidase we p r epared flavine adenine dinucleocide (FAD) from bread yeast following the Warburg-Christian's method. Apoenzyme to be added to the FAD solution we extracted from fresh human kidney following the Negelein-BrOmers method. About the coexistent system of coenzyme and prote i ne we examined the ability of desamination as the function of oxygen cosumption in the Warburg's differential manometer. Repeeting this e x periment, we could not observe any change of oxygen utilisation compared to the system which contains FAD and D, L-alanine only, but without proteine of human kidney. Such a result shows us that Negel e in-BrOmers proteine prepared from human kidney does not act as apoenzyme of aminoacidoxidase coupling with flavine ademine dinucleotide as prosthetic group.