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- W1491772630 abstract "Summary Although acetylation destroys the ability of rabbit anti-BSA to form a precipitate with BSA it was found here that it still combines with BSA to form soluble complexes. The combination was studied by electrophoretic and ultracentrifugal methods. Acetylation of 96% of the amino groups of anti-BSA γ-globulin resulted in a preparation that could still form soluble complexes with BSA. Normal rabbit γ-globulin, however, when acetylated to 86% of its amino groups, did not form soluble complexes with BSA. The failure of acetylated antibody to form a precipitate with its antigen is attributed to electrostatic repulsion effects between antibody molecules." @default.
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- W1491772630 date "1961-04-01" @default.
- W1491772630 modified "2023-09-23" @default.
- W1491772630 title "Retention of Rabbit Antibody Activity during Acetylation" @default.
- W1491772630 doi "https://doi.org/10.4049/jimmunol.86.4.452" @default.
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