Liang M N, Witt S N, McConnell H M
Department of Chemistry, Stanford University, CA 94305-5080.
J Immunol Methods. 1994 Jul 12;173(1):127-31. doi: 10.1016/0022-1759(94)90290-9.
Studies on the kinetics of antigenic peptide binding to major histocompatibility complex class II molecules have been used extensively to probe major histocompatibility complex (MHC) structure as well as to investigate the molecular mechanism of peptide recognition. Previous experiments have frequently been carried out in the presence of a cocktail of protease inhibitors to inhibit the proteolysis of MHC heterodimers. By using high performance size exclusion chromatography to measure fluorescent peptide binding to MHC protein, we have found that the addition of a commonly used mixture of protease inhibitors leads to a significant reduction in peptide binding to the class II heterodimer.
关于抗原肽与主要组织相容性复合体II类分子结合动力学的研究已被广泛用于探究主要组织相容性复合体（MHC）的结构以及研究肽识别的分子机制。先前的实验经常在蛋白酶抑制剂混合物存在的情况下进行，以抑制MHC异二聚体的蛋白水解。通过使用高效尺寸排阻色谱法来测量荧光肽与MHC蛋白的结合，我们发现添加常用的蛋白酶抑制剂混合物会导致肽与II类异二聚体的结合显著减少。
