Document Detail

Expression, high-pressure refolding and purification of human leukocyte cell-derived chemotaxin 2 (LECT2).
MedLine Citation:
PMID:  23337084     Owner:  NLM     Status:  Publisher    
Human leukocyte cell-derived chemotaxin 2 (LECT2) is a chemotactic factor for neutrophils and a 16-kDa secreted protein consisting of 133 amino acids with three intramolecular disulfide bonds. Here, we propose an efficient method for the preparation of human LECT2 using a high hydrostatic pressure (HHP, 200 MPa) refolding technique. When LECT2 was over-expressed in E. coli cells, most of LECT2 molecules became insoluble inclusion bodies (IBs). HHP was applied to the refolding of LECT2 from insoluble IBs, which dramatically improved the yield of the active LECT2. CD and NMR measurements demonstrated that the refolded LECT2 had a tertiary structure indistinguishable from the solubly expressed LECT2. In addition, both the refolded and solubly expressed LECT2 showed the same level of chemotactic activity.
Hai Zheng; Takuya Miyakawa; Yoriko Sawano; Satoshi Yamagoe; Masaru Tanokura
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-18
Journal Detail:
Title:  Protein expression and purification     Volume:  -     ISSN:  1096-0279     ISO Abbreviation:  Protein Expr. Purif.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-22     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9101496     Medline TA:  Protein Expr Purif     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2013. Published by Elsevier Inc.
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
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