[Isolation and characteristics of highly-purified phenylalanine hydroxylase from the rat liver].

Electrophoretically homogenous phenylalanine hydroxylase was isolated from rat liver tissue using a number of methods involving affinity chromatography on phenyl-Sepharose, ion exchange chromatography on DEAE-Toyoperle and hydrophobic rechromatography on phenyl-Sepharose. Molecular mass of the enzyme was equal to 50,000 Da and Km = 4.4 X 10(-3) M with phenylalanine as a substrate. The enzymatic preparations were used for immunization of rabbits and the monospecific antiserum towards phenylalanine hydroxylase was produced.