Biomedical subjects
Publications and source records attributed to C Maslet.
The chemical acetylation of RBC bearing the acquired B antigen led to the disappearance of the agglutinability by anti-B and restored the A1 specificity. The same results are obtained using RBC transformed in vitro by a Clostridium Tertium filtrate, where a deacetylase was reported.
Various anti-Cad and anti-Sda reagents were tested against a panel of Cad red cells in order to determine whether Cad and Sda antigens were identical. According to the results, although strong Sda reactivity was always found in Cad red cells, the two antigen specificities are not identical. The polyagglutinability of Cad red cells seems to be related to an anti-Cad present in all human sera but Cad, and not with anti-Sda antibody.
Nine cases of acquired B antigen were studied. By quantitative methods the variation of the A reactivity and of the number of A sites was found to be inversely related to the variation of the B reactivity. By agglutination kinetics using an immune anti-B, the acquired B reactive structure was found to differ from that of a normal B. Agglutination variation, with pH, points out to the part played by one electrically charged chemical group. No transferase galactosyl activity was found in the serum, and no B substance in the plasma. According to these results the B reactive structure must have been formed at the expense of the A reactive structure. This "acquired B" type may have arisen as a result of the action of a bacterial deacetylase, transforming the A reactive N-acetyl galactosamine into galactosamine.