Expression carrier for black porgy antibiotic peptide Hepcidin and expression product and constructing preparation method

A technology for expression vectors and expression products, which is applied in the field of construction and preparation of expression vectors, and can solve problems such as inability to meet industrialization requirements, few research reports, and complicated processes
CN101063145AActive Publication Date: 2007-10-31XIAMEN UNIV
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Patent Information

Authority / Receiving Office
CN · China
Current Assignee / Owner
XIAMEN UNIV
Publication Date
2007-10-31

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Abstract

The invention discloses an expressing carrier of black porgy antibiotic peptide Hepcidin, expressing product and preparing method, which is characterized by the following: incorporating E. coliTrc promoter, protein project improving CKS gene and procaryotic expressing carrier pTrc-CKS of histidine tag (His-Tag); connecting to black porgy Hepcidin gene; constructing pTrc-CKS / hepcidin expressing plasmid; possessing P3C enzyme cutting site; fusing six histidine on C end; getting CKS-hepcidin; purifying through C end His-Tag affinity chromatography; getting the purified product; cutting CKS with P3C enzyme in fuse protein; getting the purified Hepcidin.
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Description

technical field

[0001] The invention relates to fish gene engineering in the field of biotechnology, in particular to the construction of an expression vector of black sea bream antibacterial peptide Hepcidin with antibacterial activity and its preparation method. Background technique

[0002] Hepcidin is a family of antimicrobial peptides rich in cysteine ​​residues at the C-terminal conserved site. Their C-terminals all retain the enrichment region formed by cysteine, and CD (circular dichroism, circular dichroism) spectroscopic characteristics studies have confirmed that hepcidin has two stable β-sheet structures in phosphate buffer. It is very similar to the cystine (cystin-eknot) structure of the antibacterial polypeptide. Cysteine-rich antimicrobial peptides have been isolated from fat bodies of insects, hemolymph of molluscs and crustaceans, epithelial cells of mammals, and circulating cells such as neutrophils and macrophages. These antimicrobial peptides have acti...

Claims

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