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• W2054189087 startingPage "891" @default.
• W2054189087 abstract "Quatitative immunochemical studies of the reaction between horse and rabbit antitoxins with purified fragment A and fragment B polypeptides isolated from nicked diphtheria toxin, and with two non-toxic serologically related, mutant proteins, crm45 and crm197, have made it possible to map the locations of certain antigenic determinants along the toxin molecule. Antibodies directed against the fragment A portion of the molecule inhibit the enzymic activity of isolated fragment A and of reduced and alkylated nicked toxin in vitro, but fail to neutralize toxin in vivo. Antibodies against determinants on fragment B, especially those located on its 17,000 dalton C-terminus, have a high affinity for toxin and neutralize toxicity in vivo by preventing its attachment to the sensitive cell membrane, but do not interact with fragment A. Evidence is presented that the avidity of an antitoxin is inversely related to its anti-fragment A content. Since anti-fragment A fails to neutralize the action of toxin in vivo, maximal avidity is possible only in sera that contain no anti-fragment A. It is further suggested that most of the antigenic determinants of fragment A are masked in intact toxin, but become uncovered as a result of degradation of the more labile fragment B portion of the molecule either as a result of proteolytic action during storage in vitro, or in the animal that is being immunized." @default.
• W2054189087 created "2016-06-24" @default.
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• W2054189087 date "1972-09-01" @default.
• W2054189087 modified "2023-10-17" @default.
• W2054189087 title "An immunological study of the diphtheria toxin molecule" @default.
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• W2054189087 doi "https://doi.org/10.1016/0019-2791(72)90163-2" @default.
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