The isolation and characterization of a mouse myeloma protein with anti-dextran activity.
A myeloma protein in ascitic fluid from BALB/c mice bearing W3129 plasma cell tumors was isolated by affinity chromatography. This protein exhibits anti-dextran activity and has been obtained in highly purified form by selective adsorption on isomaltosyl-Sepharose and elution with isomaltose solution. The isomaltosyl-Sepharose was synthesized from maltose, p-aminophenyl glucoside and cyanogen bromide-activated Sepharose by a new procedure utilizing glucosyltransferase and chemical coupling reactions. Results of gel electrophoresis, isoelectrofocusing and agar diffusion experiments showed that the purified myeloma protein consisted of 6 isomeric proteins with each isomer possessing anti-dextran activity. Data from hapten inhibition studies were interpreted to show that the W3129 myeloma protein combines with terminal isomaltosyl units of branched dextrans and oligosaccharides.
D000818:Animals; D000937:Antigen-Antibody Reactions; D002846:Chromatography, Affinity; D003911:Dextrans / Q000276:immunology*; D004591:Electrophoresis, Polyacrylamide Gel; D007163:Immunosorbent Techniques; D007525:Isoelectric Focusing; D007534:Isomaltose / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D009194:Myeloma Proteins / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism
D003911:Dextrans; D009194:Myeloma Proteins; D007534:Isomaltose