Bright G M, Singh I
Division of Endocrinology, Medical University of South Carolina, Charleston 29425.
J Clin Endocrinol Metab. 1990 Jan;70(1):95-9. doi: 10.1210/jcem-70-1-95.
A quantitative assay for human adrenal autoantibodies has been developed to aid in the detection and isolation of human adrenal antigens. To define the subcellular location(s) of the antigen(s) capable of binding with these antibodies, we have quantitated both antibody binding to various adrenal subcellular fractions and the adrenal autoantibody binding inhibition caused by each subcellular fraction. To further define the subcellular location of the autoantibody binding, each fraction was assayed for organelle-specific marker enzyme activities. Enzyme activities were correlated to adrenal autoantibody binding to each fraction by linear regression. Of the materials tested, both antibody binding and inhibition of binding were most highly correlated with adrenal subcellular fractions enriched with cytochrome-c reductase and 5'-nucleotidase (r = 0.98; P less than 0.05). Thus, our data support the localization of adrenal autoantigen(s) in the microsomes, plasma membrane, or both.
已开发出一种用于检测人肾上腺自身抗体的定量测定法，以辅助检测和分离人肾上腺抗原。为了确定能够与这些抗体结合的抗原的亚细胞定位，我们对抗体与各种肾上腺亚细胞组分的结合以及每个亚细胞组分引起的肾上腺自身抗体结合抑制进行了定量。为了进一步确定自身抗体结合的亚细胞定位，对每个组分进行了细胞器特异性标记酶活性测定。通过线性回归将酶活性与肾上腺自身抗体与每个组分的结合相关联。在测试的材料中，抗体结合和结合抑制与富含细胞色素c还原酶和5'-核苷酸酶的肾上腺亚细胞组分相关性最高（r = 0.98；P小于0.05）。因此，我们的数据支持肾上腺自身抗原定位于微粒体、质膜或两者之中。
