Purification of HLA-DR molecules
- VernacularTitle:HLA-DR分子的分离纯化
- Author:
Shuai-Zheng, JIA
;
Hong-Yan, SUN
;
Xiao-Da, LIU
;
Zhi-Yan, DU
;
Quan-Li, WANG
- Publication Type:Journal Article
- From:Bulletin of The Academy of Military Medical Sciences
2001;25(1):13-16
- CountryChina
- Language:Chinese
-
Abstract:
Objective:To purify HLA-DR molecules. Methods: Anti-HLA-DR antibody L243 was purified and coupled with CNBr activated Sepharose 4B gel. Immunoaffinity column was used to purify HLA-DR molecules. Results:Twenty micrograms of HLA-DR molecules were isolated from about 5 g Epstein-Barr virus-transformed human B lymphoblastoid cell line RAJI lysates by affinity chromatography. The purified HLA-DR molecules existed in α/β heterodimers form and could bind to conformation-dependent antibody L243. These HLA-DR molecules were separated into two strands,α and β,by boiling denaturation. These results are the basis for studying MHC Ⅱ binding peptide motif and CD4＋ T cell epitopes of antigens in future.
