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- W2325500374 abstract "1) An enzyme which destroys the serological activity of blood group A substance has been purified from culture filtrate of Clostridium tertium O (H), Lea by DEAE-Sephadex A-50 column chromatography. The enzyme treatment did not produce an increase in H activity of A substance. The results indicate that the purified A-decomposing enzyme deacetylates N-acetylamino groups in blood group A substance.2) Anti-Adeac specific agglutinin which reacted with N-deacetylase treated A red cells (Addeac) was found in 40% of human sera including all ABO blood groups. In group A human sera, two kinds of agglutinin which reacted with Adeac red cells were found; one showed specific activity only to the Adeac red cells and the other cross-reacted with not only Adeac red cells, but also group B red cells. Most of group A sera contained two kinds of agglutinin, the cross-reactive as will as the specific agglutin, and some sera contained only cross-reactive agglutinin besides anti-B specific aggltinin. The Adeac specific and the cross-reactive agglutinins were found in rabbit and chicken sera immunized with N-deacetylase treated A substance.3) The agglutination reaction of anti-Adeac specific agglutinin in human sera was specifically inhibited by D-galactosamine. Reaction of cross-reactive agglutinin in group A sera was absorbed strongly by D-galactosamine and N-acetyl-D-galactosamine, and weakly by D-galactose and D-glucosamine.4) The fact that N-deacetylase treated A saliva and A substance become to inhibit the agglutination of anti-Adeac human sera with Adeac red cells indicate that the N-deacetylase treated A saliva and A substance acquired the same Adeac activity as shown in N-deacetylase treated A red cells." @default.
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- W2325500374 date "1977-01-01" @default.
- W2325500374 modified "2023-10-06" @default.
- W2325500374 title "STUDIES ON AGGLUTININ IN HUMAN SERA REACTING WITH N-DEACETYLASE TREATED BLOOD GROUP A RED CELLS (Adeac) AND A SUBSTANCES" @default.
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- W2325500374 doi "https://doi.org/10.2974/kmj1951.27.17" @default.
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