人抗-M凝集素的免疫球蛋白结构。

The immunoglobulin structure of human anti-M agglutinins.

作者信息

Smith M L, Beck M L

出版信息

Transfusion. 1979 Jul-Aug;19(4):472-4. doi: 10.1046/j.1537-2995.1979.19479250186.x.

DOI:10.1046/j.1537-2995.1979.19479250186.x

Abstract

Fifty examples of human anti-M agglutinins were subjected to reductive cleavage using both 2-mercaptoethanol (2-ME) and dithiothreitol (DTT). Thirty-nine (78%) were resistant to inactivation by sulphydryl compounds indicating IgG composition. This was confirmed by column chromatography. The remaining eleven sera were sensitive to reduction cleavage. There was no obvious association of immunoglobulin composition of the antibody with previous immune exposure to the M antigen. These results confirm observations in the literature that anti-M agglutinins are an exception to the generally expected correlation of saline agglutinating activity with IgM structure.

摘要

五十份人抗-M凝集素样本同时使用2-巯基乙醇（2-ME）和二硫苏糖醇（DTT）进行还原裂解。三十九份（78%）对巯基化合物的失活具有抗性，表明其为IgG组成。这通过柱色谱法得到了证实。其余十一份血清对还原裂解敏感。抗体的免疫球蛋白组成与先前对M抗原的免疫暴露之间没有明显关联。这些结果证实了文献中的观察结果，即抗-M凝集素是盐水凝集活性与IgM结构通常预期相关性的一个例外。