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- W2094501358 abstract "Abstract BALB/c mice were immunized with the random sequence polypeptide [Glu 60 Ala 40 ] n (GA). ∗ Spleen and lymph nodes were used to prepare T lymphocyte suspensions via nylon-wool columns. These cells were radiolabelcd with 125 I by the lactoperoxidase procedure and then ruptured by nitrogen cavitation. Membrane fragments were isolated by sucrose density centrifugation and subsequently solubilized in Triton X-100. Nonspecific material was removed by passing the solubilized membranes through an immunoadsorbent composed of d -GA (i.e. [ d -Glu 60 - d -Ala 40 ] n ) covalently bound to Sepharose 4B. The nonadherent fraction was subsequently passed through l -GA Sepharose and the adherent material eluted with 3 M NaCNS. After removal of salt and relabeling, the eluate was readsorbed onto and eluted from a fresh l -GA column. This material bound almost completely to l -GA immunoadsorbents (80–85%) but at control levels (8–10%) to immunoadsorbents composed of d -GA, d -GAT (i.e. [ d -Glu 60 - d -Ala 30 - d -Tyr 10 ] n ) or l -GAT. Polyacrylamide gel electrophoresis revealed only one component with a molecular weight of 60,000–70,000. Gel filtration chromatography in the presence of Triton X-100 indicated a higher molecular weight, probably due to aggregation and/or detergent binding. Membranes were also prepared from normal, non-immune BALB/c mice and fractionated over immunoadsorbent columns in the manner described. On the basis of incorporated radiolabel, the total amount of antigen-binding membrane recovered was 15% of that obtained in immune animals. These membranes demonstrated no specificity in binding to either l -GA or d -GA immunoadsorbents." @default.
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- W2094501358 date "1980-07-01" @default.
- W2094501358 modified "2023-09-23" @default.
- W2094501358 title "Preparation of an antigen-binding fragment from murine T lymphocyte membranes" @default.
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- W2094501358 doi "https://doi.org/10.1016/0161-5890(80)90038-3" @default.
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