A SYNTHETIC OLIGOPEPTIDE DERIVED FROM HUMAN THYROTROPIN RECEPTOR SEQUENCE BINDS TO GRAVES IMMUNOGLOBULIN AND INHIBITS THYROID STIMULATING ANTIBODY-ACTIVITY BUT LACKS INTERACTIONS WITH TSH

被引：58

作者：

MORI, T ^{[1
]}

SUGAWA, H ^{[1
]}

PIRAPHATDIST, T ^{[1
]}

INOUE, D ^{[1
]}

ENOMOTO, T ^{[1
]}

IMURA, H ^{[1
]}

机构：

[1] KYOTO UNIV,SCH MED,DIV INTERNAL MED 2,KYOTO 60601,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 178卷 / 01期

关键词：

D O I：

10.1016/0006-291X(91)91794-D

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An 11-residue oligopeptide, P-195, was synthesized to match human thyrotropin (TSH) receptor structure from No. 333 to 343 of amino acid sequence. Preincubation of 5 Graves' IgGs with P-195 up to 10 μg resulted in dose-dependent reductions of thyroid stimulating antibody (TSAb) activity. [125I] labeled P-195 was found to bind Graves' IgG. The bound radioactivity correlated significantly with their TSAb activity (N=25, r=0.587, p<0.01). A peptide having a completely reverse sequence as P-195 did not show such biological activity. The peptide did not affect TSH and thyrotropin binding inhibitor immunoglobulin (TBII) on their receptor binding nor biological activities. P-195 was concluded to have a part of TSAb binding sites. © 1991.

引用

页码：165 / 172

页数：8

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