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 2016/02
Type
Peer Review Peer reviewed
Title Halophilic metal binding protein and its His-Asp repeating peptides as fusion partner for high solubility-purification of fusion proteins
Contribution Type
Journal Bull Soc Sea Water Sci.
Journal TypeJapan
Volume, Issue, Page 70,pp.51-52
Total page number 1
Authorship Lead author
Author and coauthor Yamaguchi R, Ishibashi M, Tokunaga H, Arakawa T, Tokunaga M
Details Histidine-rich metal binding protein(HP)has been found to have high binding capacity to several heavy metal ions and was expressed in Escherichia coli cytoplasm as soluble form in large amount. Here, we employed properties of this halophilic HP as a solubility-enhancing partner protein for soluble expression and for immobilized metal ion affinity purification. We also demonstrated that a novel insertion sequence(HD50)of HP containing His-Asp repeating sequence exhibited metal binding capacity.