Evidence for the glycoprotein nature of retina glycogen

作者: Miguel A. AON , Juan A. CURTINO

DOI: 10.1111/J.1432-1033.1984.TB08138.X

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摘要: Incubation of a bovine retina membrane preparation with micromolar amounts UDP-[14C]glucose resulted in the incorporation [14C]glucose into endogenous (14)-α-glucan, insoluble trichloroacetic acid, and acidsoluble ethanol-insoluble glycogen. 1 The trichloroacetic-acid-insoluble glucan fraction migrated 2.6–3% acrylamide gels when subjected to sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS-PAGE) was rendered by digestion pronase. 2 The solubility acid-insoluble acidified organic solvent different from that amylose or glycogen similar proteins glycoproteins. 3 The contained 1.5–2.0 μ protein/100 glucose. When this analyzed SDS-PAGE only one band, which moved near top 3% gels, stained periodic acid Schiff reagent Coomassie blue. 4 The protein nature Coomassie-blue-stainable material demonstrated iodination [131I]iodide identification labeled monoiodotyrosine diiodotyrosine. The bulk label comigrated carbohydrate treatmet α-amylse decreased molecular size both stainable material. 5 Physical dissociative conditions (7.5 M urea/0.83% mercaptoethanol) following chemical tratments failed dissociate iodinated glycogen: (a) 0.1 NaOH/0.1 NaBH4 at room temperature for 24h; (b) 1 HCl methanol 50°C 10 min; (c) trifluoroacetic 6 min. 6 131I-labeled glycogenpeptide isolated after 131I-labeled protein-bound had been papain/pronase passed through Sepharose column. 7 The results suggest least part is firmly combined as single proteoglycogen molecule. Furthermore some might be present trichloroacetic-acid-precipitable proteoglucan owing its lower glucose content.

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