对免疫球蛋白E具有高亲和力的受体亚基的进一步表征。

Further characterization of the subunits of the receptor with high affinity for immunoglobulin E.

作者信息

Alcaraz G, Kinet J P, Liu T Y, Metzger H

出版信息

Biochemistry. 1987 May 5;26(9):2569-75. doi: 10.1021/bi00383a024.

Abstract

The alpha, beta, and gamma subunits of the receptor with high affinity for immunoglobulin E were isolated and their compositions assessed by direct amino acid analysis and by incorporation of radioactive precursors. The compositions show no unusual features other than a rather high content of tryptophan in the alpha chain as assessed from the incorporation studies. The results combined with future sequence data will permit unambiguous determination of the multiplicity of the chains in the receptor. Chymotryptic peptide maps of the extrinsically iodinated subunits show several similar peptides, particularly for alpha and beta. However, these putative homologies were not apparent when tryptic maps of the biosynthetically ([3H]leucine) labeled subunits were analyzed.

摘要

分离出对免疫球蛋白E具有高亲和力的受体的α、β和γ亚基，并通过直接氨基酸分析和放射性前体掺入来评估它们的组成。从掺入研究评估，这些组成除了α链中色氨酸含量相当高之外没有其他异常特征。这些结果与未来的序列数据相结合，将能够明确确定受体中链的多样性。外在碘化亚基的胰凝乳蛋白酶肽图显示出几种相似的肽，特别是α和β亚基的。然而，当分析生物合成（[3H]亮氨酸）标记亚基的胰蛋白酶肽图时，这些假定的同源性并不明显。