Expression, purification and interaction of human leukocyte antigen F and cluster of differentiation 8alpha homodimers / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 1521-1526, 2011.
Article
in Chinese
| WPRIM
| ID: wpr-304549
ABSTRACT
To obtain large quantity of human leukocyte antigen F (HLA-F) and cluster of differentiation 8alpha homodimers (CD8alphaalpha) proteins and to study their relationship, HLA-F and CD8alpha genes with rare codon in Escherichia coli were cloned using an N-terminal synonymous mutation method. High-efficiency expression protein inclusion bodies were acquired. The proteins were refolded using the dilution method and purified with gel-filtration and anion exchange chromatography. The results of gel-filtration and native-PAGE indicate that HLA-F interacts with CD8alphaalpha. This interaction may affect the binding between CD8alphaalpha and other MHC molecules to regulate immune responses. These results provide a basis for further research of HLA-F.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Recombinant Proteins
/
Histocompatibility Antigens Class I
/
CD8 Antigens
/
Escherichia coli
/
Protein Interaction Domains and Motifs
/
Protein Multimerization
/
Genetics
/
Metabolism
/
Mutation
Limits:
Humans
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2011
Type:
Article
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