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- W2019998483 abstract "Phenylalanine hydroxylase (EC 1.14.16.1) antigen and activity have been identified among proteins extracted with a buffer containing 0.4% Triton X-100 from adult human liver bioptate fraction, which was sedimented at 105,000 x g (n = 4). This enzyme fraction was designated as a 'membrane-bound form of phenylalanine hydroxylase'. It amounted to 5-15% of phenylalanine hydroxylase activity and 15-25% of phenylalanine hydroxylase antigen content. After immunoblotting two-dimensional gels, the soluble (cytoplasmic) form of phenylalanine hydroxylase antigen displayed three spots: one spot corresponded to the L-subunit with a molecular weight of 55,000, the two other spots corresponded to the H-subunit with a molecular weight of 57,000. Only the L-subunit was revealed in the membrane-bound enzyme form. Both phenylalanine hydroxylase activity and antigen were also demonstrated in extracts from human embryonic livers (n = 7). However, in this case the membrane-bound phenylalanine hydroxylase amounted to 85% of the antigen content. Subunit compositions of the enzymes were similar in adult and embryonic livers. The differences in the subunit compositions and enzyme activities of membrane-bound and cytoplasmic forms of phenylalanine hydroxylase in adults and embryos may be due to other functions of this enzyme in the hepatocyte membrane." @default.
- W2019998483 created "2016-06-24" @default.
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- W2019998483 date "1992-01-01" @default.
- W2019998483 modified "2023-09-23" @default.
- W2019998483 title "Membrane-bound phenylalanine hydroxylase of human liver" @default.
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- W2019998483 doi "https://doi.org/10.1016/s0168-8278(05)80088-1" @default.
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