Isolation,Purification and Identification of Recombinant Human Hepcidin / 微生物学通报
Microbiology
;
(12)1992.
Article
in Chinese
| WPRIM
| ID: wpr-685091
ABSTRACT
Method of isolation and purification of recombinant hepcidin was described, and the bioactivity of the protein was assayed in this paper.The oxidation of his-hepcidin was carried out in the cysteine-cystine system, and the multimers were removed through gel filtration under denaturation condition.Then the protein was refolded by continuous dilution and digested by enterokinase.The total yield of his-hepcidin before enterokinase cleavage is 50%, and the purity is above 95%.Through agar diffusion assay, the recombinant hepcidin displayed obvious antibacterial activity against B.subtilis.The LC-ESI-MS analysis of recombinant hepcidin showed that the measured molecular weight accorded with the calculated molecular weight, and the CD spectrum indicated that the secondary structure of recombinant hepcidin is similar with native hepcidin.
Full text:
Available
Index:
WPRIM (Western Pacific)
Type of study:
Diagnostic study
Language:
Chinese
Journal:
Microbiology
Year:
1992
Type:
Article
Similar
MEDLINE
...
LILACS
LIS