Improved recovery of a fusion protein containing the antigenic domain 1 of the human cytomegalovirus glycoprotein B.

Abstract:

:Heterologous expression in Escherichia coli often leads to production of the expressed proteins as insoluble and inactive inclusion bodies. The general strategy for protein recovery includes isolation and washing of inclusion bodies, solubilization of aggregated protein and refolding of solubilized protein. The process of refolding, as well as the other steps involved in inclusion body recovery, must be optimized according to the characteristics of each protein. For the development of reliable and inexpensive serodiagnostic tests, the antigenic domain 1 (AD-1) of human cytomegalovirus glycoprotein B was expressed in E. coli and a process was developed to increase recovery of the fusion protein containing AD-1. A comparison of disruption methods and different conditions involved in recovery of this fusion protein from inclusion bodies is presented. The developed method gives a high yield of the fusion protein with a purity sufficient for use in diagnostic tests.

journal_name

Biotechnol Lett

journal_title

Biotechnology letters

authors

Ferreira S,Sousa F,Queiroz JA,Domingues FC

doi

10.1007/s10529-005-0024-x

keywords:

subject

Has Abstract

pub_date

2005-08-01 00:00:00

pages

1241-5

issue

16

eissn

0141-5492

issn

1573-6776

journal_volume

27

pub_type

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