Expression, purification, and bioactivity of GST-fused v-Src from a bacterial expression system / 浙江大学学报(英文版)(B辑:生物医学和生物技术)
Journal of Zhejiang University. Science. B
; (12): 13-19, 2006.
Article
in English
| WPRIM (Western Pacific)
| ID: wpr-263230
Responsible library:
WPRO
ABSTRACT
v-Src is a non-receptor protein tyrosine kinase involved in many signal transduction pathways and closely related to the activation and development of cancers. We present here the expression, purification, and bioactivity of a GST (glutathione S-transferase)-fused v-Src from a bacterial expression system. Different culture conditions were examined in an isopropyl beta-D-thiogalactopyranoside (IPTG)-regulated expression, and the fused protein was purified using GSH (glutathione) affinity chromatography. ELISA (enzyme-linked immunosorbent assay) was employed to determine the phosphorylation kinase activity of the GST-fused v-Src. This strategy seems to be more promising than the insect cell system or other eukaryotic systems employed in earlier Src expression.
Full text:
Available
Database:
WPRIM (Western Pacific)
Main subject:
Saccharomyces cerevisiae
/
Bacterial Proteins
/
Recombinant Fusion Proteins
/
Protein Engineering
/
Chemistry
/
Oncogene Protein pp60(v-src)
/
Genetics
/
Glutathione Transferase
/
Metabolism
/
Methods
Language:
English
Journal:
Journal of Zhejiang University. Science. B
Year:
2006
Document type:
Article