Antigen-specific T lymphocyte clones. III. Papain splits purified T suppressor molecules into two functional domains
Antigen-specific T lymphocyte clones. III. Papain splits purified T suppressor molecules into two functional domains
复制标题
抗原特异性 T 淋巴细胞克隆。
DOI：
--
复制
发表时间：
1982
影响因子：
15.3
通讯作者：
H. Cantor
中科院分区：
文献类型：
--
作者：
M. Fresno;L. McVAY;H. Cantor
从t抑制因子（T-suppressor, Ts）克隆中纯化的分子（70,000 mol wt）与绵羊红细胞糖蛋白结合，特异性抑制对该抗原的反应。木瓜蛋白酶将纯化的70000 mol wt的Ts分子分成两个多肽：45000 mol wt和24000 mol wt。45,000 mol wt的肽非特异性地抑制抗体对几种抗原的反应，缺乏抗原结合活性。24000 mol wt的肽不抑制而保留抗原结合活性。结果表明，木瓜蛋白酶将Ts分子分裂成一个负责功能的“恒定”区域和一个负责抗原结合的“可变”区域。由于70000 mol wt分子与抗原的结合也导致45000 mol wt亚基的释放，这种切割可能允许特定于一种决定因素的Ts分子抑制对复杂外源蛋白的免疫。
Purified molecules (70,000 mol wt) from a T-suppressor (Ts) clone bind to sheep erythrocyte glycophorin and specifically suppress the response to this antigen. Papain splits purified 70,000-mol wt Ts molecules into two peptides: mol wt 45,000 and 24,000. The 45,000-mol wt peptide nonspecifically suppresses antibody response to several antigens and lacks antigen-binding activity. The 24,000-mol wt peptide does not suppress but retains antigen-binding activity. The results indicate that papain splits the Ts molecule into a "constant" region responsible for function and a "variable" region responsible for antigen-binding. Since binding of the 70,000-mol wt molecule to antigen also results in release of the 45,000 mol wt subunit, this cleavage may allow Ts molecules specific for one determinant to suppress immunity to complex foreign proteins.