[Isolation of inactive phenylalanine hydroxylase from autopsy specimens of human liver].
An electrophoretically homogeneous protein has been isolated from human liver autoptats, using a procedure employed for the isolation of phenylalanine hydroxylase from rat liver. The procedure includes chromatography of liver extracts on phenyl-Sepharose and subsequent purification on DEAE-Toyopearl. The activity of phenylalanine hydroxylase in the autoptats was markedly decreased in comparison with that in bioptats. The isolated protein possessed no enzymatic activity. However, the subunit composition of the protein, the molecular masses of protein subunits (55 and 57 kD) and the amino acid composition were close to those of the human enzyme. Antibodies to the protein inhibited the phenylalanine hydroxylase activity in human liver bioptats and weakly inhibited the rat enzyme. The experimental results suggest that the structural organization of phenylalanine hydroxylase does not alter as a result of the loss of enzymatic activity in cadaverous human liver.
D000596:Amino Acids / Q000032:analysis; D001344:Autopsy; D001706:Biopsy; D002852:Chromatography, Ion Exchange; D006801:Humans; D007122:Immunoelectrophoresis; D008099:Liver / Q000201:enzymology*; D010651:Phenylalanine Hydroxylase / Q000037:antagonists & inhibitors / Q000302:isolation & purification*
D000596:Amino Acids; D010651:Phenylalanine Hydroxylase
Poluchenie neaktivnogo belka fenilalaningidroksilazy iz autoptatov pecheni cheloveka.