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- W4313310173 abstract "Abstract An unusual patient with multiple myeloma and hyperlipidemia provided the basis for study of the chemistry of lipid binding by her myeloma protein. Lipid-free M protein prepared by ultracentrifugation and gel chromatography existed as IgA κ monomers and disulfide-linked dimers which were used for serologic, gel diffusion and proteolytic digestion studies. Native plasma, lipid-free plasma and purified M protein reacted in agar diffusion with α- and β-lipoprotein. The plasma also agglutinated RBC of sheep, but not those of man or other species. Inhibition of agglutination by the isolated M protein was strongest with choline, which at 0.0001 µg/ml reduced the titer from 1:2048 to 1:256. Less marked inhibition was noted with lysolecithin, phosphorylcholine and sphingomyelin. Pepsin digestion of the M protein produced serologically inactive fragments. Neither agglutination nor inhibition of agglutination was produced by H or L chains. Apparently the IgA protein binds free lipids, lipoproteins or sheep RBC through choline side chains." @default.
- W4313310173 created "2023-01-06" @default.
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- W4313310173 date "1971-09-01" @default.
- W4313310173 modified "2023-10-16" @default.
- W4313310173 title "Hyperlipidemic Myelomatosis" @default.
- W4313310173 doi "https://doi.org/10.4049/jimmunol.107.3.926.b" @default.
- W4313310173 hasPublicationYear "1971" @default.
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