摘要
目的:根据60kDSSA抗原分子不同表位的氨基酸序列,人工合成多倍体寡肽抗原表位(multipleantigenicpeptides,MAPs),以检测这些表位的免疫特性。方法:用MAPs做亲和层析柱,用抗SSA抗体的病人血清过柱,纯化抗MAPs抗体。这些纯化后的抗MAPs抗体可与60kDSSA抗原及MAPs反应。这种反应能被60kDSSA抗原及相对应的MAPs抑制。以MAPs做抗原检测67份具有抗SSA抗体的血清。结果:67份病人血清中,63份阳性,阳性率94%,这些血清结合的MAPs不同,可以从1至20个MAPs不等。结论:研究表明,60kDSSAMAPs保留了60kDSSA抗原的抗原性。
Objective:According to the different 60 kD human SSA antigenic polypeptide amino acid sepuences multiple antigenic peptides (MAPs) were synthesized to test the immunity of these antigenic epitope.Methods:AntiMAPs antibodies were purified by passing patient sera with antiSSA antibodies through affinity chromatography columns that were linked with selected SSAMAPs.These purified antibodies could respond to 60 kD human SSA antigen and relevant SSAMAPs.Sera with antiSSA antibodies of 67 patients were tested.Results:Of 67 patient sera,63 (94%) could bind to SSAMAPs and they could bind epitopes 1 to 20.Conclusion:It indicates that 60 kD human SSAMAPs keep the native molecular antigenicity.
出处
《中华风湿病学杂志》
CAS
CSCD
1998年第1期5-9,共5页
Chinese Journal of Rheumatology