Single-step purification of recombinant hepatitis B core antigen Y132A dimer from clarified Escherichia coli feedstock using a packed bed anion exchange chromatography-Reference-Cited by-同舟云学术

Single-step purification of recombinant hepatitis B core antigen Y132A dimer from clarified Escherichia coli feedstock using a packed bed anion exchange chromatography

Published:2018-06 Issue: Volume:69 Page:208-215
ISSN:1359-5113
Container-title:Process Biochemistry
language:en
Short-container-title:Process Biochemistry

Author:

Lim Swee Lu,Ng Hon Wei,Akwiditya Made Angga,Ooi Chien Wei,Chan Eng-Seng,Ho Kok Lian,Tan Wen Siang^ORCID,Chua Gek Kee^ORCID,Tey Beng Ti^ORCID

Funder

School of Engineering and Advanced Engineering Platform (AEP)

Monash University Malaysia under the Higher Degree Research (HDR) Scholarship

Fundamental Research Grant Scheme (FRGS) Ministry of Higher Education, Malaysia

Publisher

Elsevier BV

Subject

Applied Microbiology and Biotechnology,Biochemistry,Bioengineering

Reference47 articles.

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4. Conformational changes in the hepatitis B virus core protein are consistent with a role for allostery in virus assembly;Packianathan;J. Virol.,2010

5. Thermodynamic origins of protein folding allostery, and capsid formation in the human hepatitis B virus core protein;Alexander;Proc. Natl. Acad. Sci.,2013

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