Shulman S, Centeno E, Milgrom F, Witebsky E
Immunology. 1965 Jun;8(6):531-8.
Extracts of rabbit adrenal tissue, containing an adrenal-specific antigen able to elicit the formation of autoantibody, have been characterized physically and chemically. The extinction coefficient was shown to be 10.3 at 280 mμ. Ultracentrifugal analysis revealed a group of components; the predominant one was a 3.9S boundary. Additional components had sedimentation coefficients of 6.6S, 10.0S, 11.8S and 18.1S. Starch block electrophoresis was unsuccessful in providing significantly purified antigen. There was a suggestion of a possible occurrence of two antigens. Some degree of fractionation was achieved by salting-out with ammonium sulphate. The antigenic material was associated with the fraction precipitating between 0.00 and 1.50 M of this salt. These studies also provided some evidence that the antigen was associated with the 6.6S sedimenting component. Enzymic digestion with chymotrypsin readily caused destruction of the activity, indicating that the antigen is essentially a protein.
已对含有能引发自身抗体形成的肾上腺特异性抗原的兔肾上腺组织提取物进行了物理和化学表征。在280 mμ处,消光系数显示为10.3。超速离心分析揭示了一组组分;主要的一个是3.9S界峰。其他组分的沉降系数为6.6S、10.0S、11.8S和18.1S。淀粉块电泳未能显著纯化抗原。提示可能存在两种抗原。通过硫酸铵盐析实现了一定程度的分级分离。抗原物质与在该盐0.00至1.50 M之间沉淀的级分相关。这些研究还提供了一些证据,表明该抗原与6.6S沉降组分相关。用胰凝乳蛋白酶进行酶消化很容易导致活性破坏,表明该抗原本质上是一种蛋白质。