Rui Yamaguchi
   Department   Kumamoto Health Science University  Department of Medical Technology, Faculty of Health Science
   Kumamoto Health Science University Graduate School  Division of Health Sciences, Graduate School of Health Sciences
   Position   Associate Professor
Language English
Publication Date 2012/01
Type
Peer Review Peer reviewed
Title Halophilic properties of metal binding protein characterized by high histidine content from Chromohalobacter salexigens DSM3043.
Contribution Type
Journal Protein J.
Journal TypeAnother Country
Volume, Issue, Page 31,pp.175-183
Total page number 8
Authorship Lead author
Author and coauthor Yamaguchi R, Arakawa T, Tokunaga H, Ishibashi M, Tokunaga M.
Details Periplasmic metal binding protein characterized by high histidine content was cloned from moderate halophile, Chromohalobacter salexigens. The protein, termed histidine-rich metal binding protein (HP), was expressed in and purified from E. coli as a native form. HP bound to Ni- and Cu-loaded chelate columns with high affinity, and Co- and Zn-columns with moderate affinity. Although the secondary structure was not grossly altered by the addition of 0.2–2.0 M NaCl, the thermal transition pattern was considerably shifted to higher temperature with increasing salt concentration.