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• W2040996894 abstract "Abstract The binding of the optical enantiomorphs, poly(Glu 60 Ala 30 Tyr 10 ) ( l -GAT) and poly( d Glu 60 d Ala 30 d Tyr 10 ) ( d -GAT), to rat peritoneal exudate ribonucleoprotein (RNP) was investigated. the l -GAT copolymer exhibited an average of twenty times the binding of the d -GAT copolymer. This difference was paralleled by a difference in the degree of conversion of the two enantiomorphs to a trichloroacetic acid (TCA)-soluble form. On the other hand, no discrimination in binding was observed when radiation-degraded fragments of both copolymers were used. These results support the conclusion that peritoneal exudate cells must carry out a sterospecific degradation step before antigen can bind to the RNP molecule. Because the quantitative difference inbinding of the two optical enantiomorphs seemed to correlate with their difference in immunogenicity, further experiments were performed to determine if such a correlation were a general rule. Conversion of the d -GAT copolymer to a more immunogenic form by complexing it with methylated bovine serum albumin (MBSA) did not increase the amount of binding to the RNP molecule. In addition, the binding of an immunogenic, neutral analogue of the l -GAT copolymer, poly[N 5 -(3-hydroxypropyl)Gln 60 Ala 30 Tyr 10 ], was less than the binding of the weakly immunogenic d -GAT copolymer. Although attachment in all four cases was correlated with the amount of TCA-soluble fragments, no definite quantitative correlation between immunogenicity and binding to the macrophage RNP could be established. However, these results do not preclude a role for the RNP molecule in the induction of an immune response as factors other than the absolute quantitative amount of binding might be important." @default.
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• W2040996894 date "1972-06-01" @default.
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• W2040996894 title "Binding of synthetic copolymers to the macrophage ribonucleoprotein" @default.
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• W2040996894 doi "https://doi.org/10.1016/0019-2791(72)90246-7" @default.
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