Phosphate-buffered native gel electrophoresis of E-Coli H-NS
- Authors
- Yook, Ji-Hwan; Kang, Choong-Min; Kim, Woo-Yeon
- Issue Date
- Oct-2016
- Publisher
- SPRINGER
- Keywords
- Histone-like nucleoid structuring protein; Modification; Native gel electrophoresis
- Citation
- APPLIED BIOLOGICAL CHEMISTRY, v.59, no.5, pp 677 - 679
- Pages
- 3
- Journal Title
- APPLIED BIOLOGICAL CHEMISTRY
- Volume
- 59
- Number
- 5
- Start Page
- 677
- End Page
- 679
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/1759
- DOI
- 10.1007/s13765-016-0214-3
- ISSN
- 2468-0834
2468-0842
- Abstract
- Histone-like nucleoid structuring protein (H-NS) is a global regulator in enteric bacteria and other bacteria. It has been reported that H-NS has no modifications for its activity. Even though H-NS is called histone-like protein, it is acidic, contrary to the basic eukaryotic histones. Here, we report that there were mobility differences for various sources of H-NS seen in sodium phosphate-buffered native gel electrophoresis. We examined various native gel electrophoresis conditions using the wild-type E. coli (MG1655), three H-NS mutants (two were H-NS knockout mutants), and the E. coli BL21 overexpressing H-NS (BL21 (DE3)/pPD3).
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- Appears in
Collections - College of Biotechnology & Natural Resource > Department of Systems Biotechnology > 1. Journal Articles
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