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One-step extraction of functional recombinant aquaporin Z from inclusion bodies with optimal detergent.

Abstract：

:Aquaporins are integral membrane channel proteins found in all kingdoms of life. The Escherichia coli aquaporin Z (AqpZ) has been shown to solely conduct water at high permeability. Functional AqpZ is generally purified from the membrane fraction. However, the quantity of the purified protein is limited. In this study, a new method is developed to achieve high yield of bioactive AqpZ protein. A mild detergent n-dodecyl-β-D-maltopyranoside (DDM) was used to solubilize the over-expressed insoluble AqpZ from inclusion bodies without a refolding process. The recovered AqpZ protein showed high water permeability comparable with AqpZ obtained from the membrane fraction. In this way, the total yield of bioactive AqpZ has been increased greatly, which will facilitate the structural and functional characterization and future applications of AqpZ.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Wang L,Zhou H,Li Z,Lim TK,Lim XS,Lin Q

doi

10.1016/j.pep.2015.08.014

subject

Has Abstract

pub_date

2015-11-01 00:00:00

pages

146-52

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(15)30034-6

journal_volume

115

pub_type

杂志文章

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