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用与热聚集γ球蛋白的IgG抗体复合的荧光素化葡萄球菌蛋白A分析单核细胞表面。

Analysis of mononuclear cell surfaces with fluoresceinated staphylococcal protein A complexed with IgG antibody of heat-aggregated gamma-globulin.

作者信息

Ades E W, Phillips D J, Shore S L, Gordon D S, LaVia M G, Black C M, Reimer C B

出版信息

J Immunol. 1976 Dec;117(6):2119-23.

PMID:62807
Abstract

Fluorescein-conjugated staphylococcal protein A (SPA) was complexed with either: 1) heat-aggregated IgG, 2) B cell specific antibody, or 3) T cell specific antibody and then used for an immunofluorescent analysis of mononuclear cell surfaces. Cellular Fc receptors failed to recognize the Fc region of aggregated IgG that had been blocked by SPA. Moreover, fluoresceinated SPA that had been complexed either with anti-Fab (B-cell specific) or T cell-specific antisera prevented the nonspecific binding of these reagents to the IgG-Fc receptors on mononuclear cells, thereby permitting the latter to be properly identified as B or T lymphocytes. In addition, when unconjugated SPA was added to presensitized target cells in a test for antibody-dependent cell-mediated cytotoxicity, cytolysis was abrogated.

摘要

将荧光素偶联的葡萄球菌蛋白A(SPA)与以下物质复合:1)热聚集的IgG、2)B细胞特异性抗体或3)T细胞特异性抗体,然后用于单核细胞表面的免疫荧光分析。细胞Fc受体无法识别已被SPA阻断的聚集IgG的Fc区域。此外,与抗Fab(B细胞特异性)或T细胞特异性抗血清复合的荧光素化SPA可防止这些试剂与单核细胞上的IgG-Fc受体发生非特异性结合,从而使后者能够被正确鉴定为B淋巴细胞或T淋巴细胞。此外,在抗体依赖性细胞介导的细胞毒性试验中,当将未偶联的SPA添加到预先致敏的靶细胞中时,细胞溶解作用被消除。

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