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- W2012173815 abstract "1. A particulate enzyme preparation obtained from bovine retina transfers N-[3H]acetylneuraminic acid ([3H]NANA) from CMP N-[3H]acetylneuraminic acid to an endogenous acceptor. It also incorporates [14C]galactose. 2. The evidence indicates a sequential addition of galactose and NANA to the same carbohydrate chain of the acceptor. 3. The transfer of [3H]NANA is stimulated by the addition of unlabeled UDP-galactose to incubation mixtures, but not by other sugar nucleotides. 4. The [3H]NANA transfer shows no metal requirement. The galactose transfer and the UDP-galactose-stimulated [3H]NANA transfer both require Mn2+. Mg2+ fails to replace Mn2+. 5. The amount of [14C]galactose transferred is always greater than the increment in [3H]NANA tranfer caused by the addition of UDP-galactose. 6. Labeled products remain bound to the particulate enzyme but can be solubilized with deoxycholate. Pronase digestion converts these products from trichloroacetic acid-insoluble proteins to trichloroacetic acid-soluble peptides. 7. Neuraminidase releases most of the [3H]NANA from the [3H]NANA-labeled peptide. However, a NANA-substituted [14C]galactose-labeled peptide resist β-galactosidase treatment unless first treated with neuraminidase." @default.
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- W2012173815 date "1968-05-01" @default.
- W2012173815 modified "2023-10-18" @default.
- W2012173815 title "Incorporation of d-[14C]galactose and N-[3H]-acetylneuraminic acid into glycoprotein by particles from bovine retina" @default.
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- W2012173815 doi "https://doi.org/10.1016/0304-4165(68)90130-x" @default.
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