Summary The reaction of antiglobulin serum with globulin fixed to erythrocytes in a non‐immunologic fashion was studied using I131 labeled antiglobulin sera. These studies revealed: 1. Rabbit globulin fractions containing anti‐human globulin antibody fixed to erythrocytes irrespective of prior exposure to anti‐D (Rho) and the D (Rho) positive or negative state of the erythrocytes. 2. Rabbit anti‐human globulin antibody fixed to human erythrocytes coated nonimmunologically with human globulin. This is a nonagglutinating reaction. 3. Human globulin fixed in a nonimmunologic fashion to erythrocytes could be eluted and would react with anti‐human globulin antibody. 4. Rabbit anti‐human globulin antibody fixed to erythrocytes was unable to induce agglutination when incomplete anti‐D (Rho) was subsequently fixed to the cell. These studies indicate that the agglutination of erythrocytes coated with incomplete antibody by antiglobulin sera is dependent on the molecular conformation of incomplete antibody. The site of primary importance in inducing agglutination appeared to be the incomplete antibody‐erythrocyte linkage. Résumé La réaction du sérum anti‐globuline avec la globuline fixée non immunologiquement aux érythrocytes a été étudiée au moyen de sérums anti‐globuline marqués B l'iode131, Ces études ont révélé: 1. La fraction de globuline de lapin contenant l'anticorpe anti‐globuline humaine se he aux érythrocytes indépendamment d'une mise en contact préalable avec de l'anti‐D (Rho) d'érythrocytes D (Rho) positif ou négatif. 2. L'anticorps de lapin anti‐globuline humaine se fixe aux érythrocytes humahs chargés non immunologiquement avec des globulines humaines. Il n'y a pas de réaction d'agglutination. 3. Les globulines bumaines fixées non immunologiquement aux érythrocytes peuvent être élués et réagiesent avec l'anticorps anti‐globuline humaine. 4. L'anti‐corps de lapin anti‐globuline humaine fixé aux érythrocytes est incapable de provoquer une agglutination quand de l'anti‐D (Rho) incomplet est ensuite mis en contact avec ces érythrocytes. Ces études démontrent que l'agglutination par des sérums anti‐globuline d'érythrocytes chargés par des anticorps incomplets est dépendant de la constitution moléculaire de I'anticorps incomplet. Le phénomène de première importance pour la mise en branle de l'agglutination semble donc être l'accouplement de l'érythrocyte avec l'anticorps incomplet. Zusammenfassung Die Reaktion von Antiglobulinserum mit Globulin, welches nicbt immunologisch an die Erythrozytenoberfläche fixiert war, wurde mit I131 markierten Antiglobulin‐seren untersucht. Diese Untersuchungen ergaben folgendes: 1. Kaninchenglobulinfraktionen, welche Anti‐Human‐Globulin‐Antikörper enthielten, wurden an die Erythrozytenoberfiäche fixiert; dabei war es gleichgültig, ob die Zellen vorgängig mit Anti‐D(Rbo) behandelt worden waren oder ob es sich um D(Rho) positive oder negative Erythrozyten handelte. 2. Anti‐Human‐Globulinseren vom Kaninchen wurden von menschlicben Erythrozyten, die nicht‐immunologisch mit menschlichem G...
Summary The pretreatment of erythrocytes with bromelin, a proteolytic enzyme, results in a 2-to 3-fold increase in globulin coating the erythrocyte surface. This increased number of globulin molecules is not responsible for the agglutination of saline suspended erythrocytes by incomplete antibody. The pretreatment of erythrocytes with tannic acid increased the number of γ-globulin molecules coating erythrocytes. This increased number of globulin molecules is not responsible for the agglutination of γ-globulin-coated erythrocytes by antiglobulin serum. Neither proteolytic enzymes nor tannic acid function in hemagglutination procedures by inducing the coating of erythrocytes with a globulin molecule. Rather, by surface changes, they permit a normally nonagglutinating reaction to result in agglutination. It is postulated that the incomplete antibody has a potentially bivalent nature. The function of enzymatic treatment in converting incomplete antibodies to complete acting substances might well be the removal of steric obstructions resulting from the disposition of antigen and incomplete antibody sites.
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