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
en Zh
| WPRIM
| ID: wpr-304549
Biblioteca responsable:
WPRO
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.
Texto completo:
1
Base de datos:
WPRIM
Asunto principal:
Proteínas Recombinantes
/
Antígenos de Histocompatibilidad Clase I
/
Antígenos CD8
/
Escherichia coli
/
Dominios y Motivos de Interacción de Proteínas
/
Multimerización de Proteína
/
Genética
/
Metabolismo
/
Mutación
Límite:
Humans
Idioma:
Zh
Revista:
Chinese Journal of Biotechnology
Año:
2011
Tipo del documento:
Article