Purification of HLA-DR molecules / 军事医学科学院院刊
Bulletin of The Academy of Military Medical Sciences
;
(6): 13-16, 2001.
Article
in Chinese
| WPRIM
| ID: wpr-643046
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Language:
Chinese
Journal:
Bulletin of The Academy of Military Medical Sciences
Year:
2001
Type:
Article
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