Conversion of the human blood group H antigen to A antigen in vitro.
A-transferase (N-acetylgalactosaminyl transferase) was purified from human group A plasma using Sepharose 4B affinity chromatography. Human anti-A antibodies were purified from human serum by adsorption to an immunosorbent column and heat elution in order to detect the A antigen. Conditions appropriate for the development of the A antigen on O red cells were examined and several buffer systems were found to be equally effective. Expression of the developed A antigen was found to be similar to that on group A red cells, indicating that the system in vitro has similar activity to the system in vivo. The H antigen from human saliva was coupled to Sepharose 4B or adsorbed to a nitrocellulose membrane. The A antigen was able to be developed on these materials by the action of group A-transferase. The procedures enabled the identification in vitro of sugar-transferase activities which can be useful in studies within the A,B,H antigen system or other carbohydrate antigen system.
Yang
N
N
Department of Biological Sciences, Newcastle University, New South Wales, Australia.
Boettcher
B
B
D000017:ABO Blood-Group System / Q000097:blood / Q000378:metabolism*; D000372:Agglutination Tests; D000906:Antibodies; D002845:Chromatography; D000939:Epitopes / Q000097:blood / Q000378:metabolism*; D004912:Erythrocytes / Q000276:immunology / Q000378:metabolism; D005700:Galactosyltransferases / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D017350:N-Acetylgalactosaminyltransferases; D011993:Recombinant Fusion Proteins; D012463:Saliva / Q000201:enzymology / Q000378:metabolism
D000017:ABO Blood-Group System; D000906:Antibodies; D000939:Epitopes; D011993:Recombinant Fusion Proteins; D005700:Galactosyltransferases; D017350:N-Acetylgalactosaminyltransferases; C003742:UDPgalactosamine-galactose acetylgalactosaminyltransferase