Differences in Epitope Restriction of Autoantibodies to Native Human Insulin (IAA) and Antibodies to Heterologous Insulin (IA)
Differences in Epitope Restriction of Autoantibodies to Native Human Insulin (IAA) and Antibodies to Heterologous Insulin (IA)
复制标题
天然人胰岛素 (IAA) 自身抗体和异源胰岛素 (IA) 抗体表位限制的差异
作者:
J. Diaz;T. Wilkin
The binding profiles of insulin autoantibodies (IAA) and insulin antibodies (IA) to highly purified species variants and fragments of insulin were studied in direct immunospecific enzyme-linked immunosorbent assay (ELISA) and indirect absorption experiments with insulins covalently coupled to Sepharose beads. Five of 10 lAA-containing sera from insulin-naive nondiabetics that bound whole human (H) insulin did not bind whole porcine (P) or whole bovine (B) insulins. These sera bound H insulin B-chain but not P B-chain or desalanated P insulin, suggesting they were dependent on the presence of threonine B30. The other 5 IAA-containing sera bound H, P, B, and desalanated porcine insulins, but only 1 bound isolated B-chains. All 10 IA-containing sera from insulin-treated diabetics bound H, P, B, and desalanated P insulins, but only 1 bound to human (and porcine) B-chain. Further binding studies with ovine, rabbit, rat, and guinea pig insulins confirmed the H (threonine B30) specificity of the 5 IAA-containing sera. B30 residues do not appear to be dominant, however, when insulin is administered exogenously. Instead, IA bind predominantly to Achain or conformational determinants involving both chains. Scatchard analysis of a representative H insulin-specific IAA serum suggested that it contained a single binding affinity, whereas analysis of a representative IA-diabetic serum suggested it contained several different affinities.
DOI:
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发表时间:
1983
期刊:
Journal of immunology (Baltimore, Md. : 1950)
影响因子:
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作者:
Bender,TP;Schroer,J;Claflin,JL
通讯作者:
Claflin,JL