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- W2074092020 abstract "Abstract Isolated bovine rod outer segment preparations catalyze the transfer of galactose and fucose from the respective sugar nucleotides to rhodopsin. The apparent K m for UDP-galactose is 4·2 μ m and for GDP fucose, 4·0 μ m . The pH optima are both 6·3. The transfer of galactose is stimulated somewhat by 0·06% Triton X-100, whereas higher concentrations inhibit. ATP (0·2 m m ) stimulates galactose transfer and can be replaced by any nucleoside di- or triphosphate except UDP and UTP, which inhibit. Nucleoside monophosphates, including UMP, neither stimulate nor inhibit, therefore the UDP and UTP inhibition is not simply competition by uridine nucleotides for the UDP galactose binding site on the transfer enzyme. Rather, the inhibition suggests the reversal of the formation of a lipid intermediate in the transfer of galactose to rhodopsin. Retinyl phosphate enhances the transfer reaction and may represent the lipid acceptor. Fucose transfer is stimulated to a lesser extent by Triton and by nucleoside di- and triphosphates. However, guanosine nucleotides including GMP, uniformly inhibit the transfer, probably by direct competition with the GDP-fucose binding site. Higher Triton concentrations do not inhibit the fucose transfer. The evidence suggests that fucose transfer does not involve a lipid carrier." @default.
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- W2074092020 date "1978-02-01" @default.
- W2074092020 modified "2023-10-18" @default.
- W2074092020 title "Characteristics of galactosyl and fucosyl transfer to bovine rhodopsin" @default.
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- W2074092020 doi "https://doi.org/10.1016/0014-4835(78)90117-3" @default.
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