Clostridium perfringens alpha-N-acetylgalactosaminidase blood group A2-degrading activity.
Enzymic modification of type A(2) erythrocyte membranes with Clostridium perfringens alpha-N-acetylgalactosaminidase was investigated. An ELISA demonstrated hydrolysis of type A(2) epitopes under conditions of red-blood-cell collection and storage. The enzyme hydrolysed the terminal N-acetyl-alpha-D-galactosamine from the blood type A(2) antigen, producing H antigen, blood group O, which is universally compatible in the ABO system. The enzyme was active in common red-cell preservative solutions at pH 6.4-7.0, at 4 degrees C, at ionic strengths found in stored red cell units and in the presence of type A plasma. These data imply that the C. perfringens alpha-N-acetylgalactosaminidase might be added directly to packed A(2) red-blood-cell units for enzymic conversion to blood type O. Further studies are warranted.
Hsieh
Hsin-Yeh
HY
Department of Pathology and Anatomical Sciences, University of Missouri-Columbia, M263 Medical Science Building, One Hospital Drive, Columbia, MO 65212, U.S.A.
Smith
Daniel
D
D000017:ABO Blood-Group System / Q000276:immunology*; D000911:Antibodies, Monoclonal / Q000276:immunology / Q000378:metabolism; D000941:Antigens / Q000378:metabolism*; D003016:Clostridium perfringens / Q000201:enzymology*; D004797:Enzyme-Linked Immunosorbent Assay / Q000379:methods*; D004910:Erythrocyte Membrane / Q000276:immunology* / Q000378:metabolism*; D006596:Hexosaminidases / Q000378:metabolism*; D006801:Humans; D013696:Temperature; D048809:alpha-N-Acetylgalactosaminidase
D000017:ABO Blood-Group System; D000911:Antibodies, Monoclonal; D000941:Antigens; D006596:Hexosaminidases; C482722:NAGA protein, human; D048809:alpha-N-Acetylgalactosaminidase