Mori T, Sugawa H, Piraphatdist T, Inoue D, Enomoto T, Imura H
Department of Laboratory Medicine, Kyoto University School of Medicine, Japan.
Biochem Biophys Res Commun. 1991 Jul 15;178(1):165-72. doi: 10.1016/0006-291x(91)91794-d.
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 micrograms 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 less than 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.
合成了一种由11个残基组成的寡肽P-195,其氨基酸序列与人类促甲状腺激素(TSH)受体结构的第333至343位相匹配。将5种格雷夫斯病(Graves')免疫球蛋白(IgG)与高达10微克的P-195预孵育,导致甲状腺刺激抗体(TSAb)活性呈剂量依赖性降低。发现[125I]标记的P-195能与格雷夫斯病IgG结合。结合的放射性与它们的TSAb活性显著相关(N = 25,r = 0.587,p < 0.01)。一种氨基酸序列与P-195完全相反的肽不具有这种生物学活性。该肽对TSH及其受体结合以及促甲状腺素结合抑制免疫球蛋白(TBII)的生物学活性均无影响。得出结论,P-195具有TSAb结合位点的一部分。