作者: V N Schumaker , M T Robinson , L K Curtiss , R Butler , R S Sparkes
DOI: 10.1016/S0021-9258(20)82160-7
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摘要: Immunochemical polymorphism among human low density lipoproteins (LDL) isolated from different individuals was demonstrated through reduced binding of three monoclonal antibodies to some individual LDL using a solid phase radioimmunoassay. These are members larger group previously shown bind specifically apoprotein B ( Curtiss , L.K., and Edgington T. S. (1982) J. Biol. Chem. 257, 15213-15221; Tsao B.P., L. K., T.S. 15222-15228). Those which distinguished bound the same or adjacent epitopes on LDL, for they were mutually exclusive in competitive experiments. Binding unaffected by treatment with neuraminidase, mixture glycosidases, competing glycoproteins; thus, carbohydrate moiety did not appear influence epitope recognized these antibodies. When studied, phenotypes recognized; corresponded strong, weak, intermediate This division into is result genetic polymorphism; indeed, data fit model consisting two co-dominant alleles, then correspond homozygotes heterozygote. The classical Ag antigen phenotype determined 10 who also studied antibodies, no correspondence found between five presumptive allelic pairs, x/y, a1/d, c/g, t/z, h/i, site All discussed, it concluded that most likely explanation difference recognition forms an alteration amino acid sequence resulting slightly configuration single domain containing