A novel protein refolding method using a zeolite

Hiroyuki Chiku; Akiko Kawai; Toyotaka Ishibashi; Masahide Takehara; Takuro Yanai; Fujio Mizukami; Kengo Sakaguchi

doi:10.1016/j.ab.2005.10.032

A novel protein refolding method using a zeolite

Hiroyuki Chiku, Akiko Kawai, Toyotaka Ishibashi, Masahide Takehara, Takuro Yanai, Fujio Mizukami, Kengo Sakaguchi^*

^*Corresponding author for this work

Research output: Contribution to journal › Journal Article › peer-review

20 Citations (Scopus)

Abstract

We have succeeded in developing a simple and effective protein refolding method using the inorganic catalyst, β-zeolite. The method involves the adsorption of proteins solubilized with 6 M guanidine hydrochroride from inclusion body (IB) preparations onto the zeolite. The denaturant is then removed, and the proteins in the IBs are released from the zeolite with polyoxyethylene detergent and salt. All of the IBs tested (11 different species) were successfully refolded under these conditions. The refolded proteins are biochemically active, and NMR analysis of one of the proteins (replication protein A 8) supports the conclusion that correct refolding does occur. Based on these results, we discuss the refolding mechanism.

Original language	English
Pages (from-to)	307-314
Number of pages	8
Journal	Analytical Biochemistry
Volume	348
Issue number	2
DOIs	https://doi.org/10.1016/j.ab.2005.10.032
Publication status	Published - 15 Jan 2006
Externally published	Yes

Keywords

Denaturant
Detergent
Inclusion body
Polyethylene glycol
Refolding
Zeolite

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10.1016/j.ab.2005.10.032

Cite this

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title = "A novel protein refolding method using a zeolite",

abstract = "We have succeeded in developing a simple and effective protein refolding method using the inorganic catalyst, β-zeolite. The method involves the adsorption of proteins solubilized with 6 M guanidine hydrochroride from inclusion body (IB) preparations onto the zeolite. The denaturant is then removed, and the proteins in the IBs are released from the zeolite with polyoxyethylene detergent and salt. All of the IBs tested (11 different species) were successfully refolded under these conditions. The refolded proteins are biochemically active, and NMR analysis of one of the proteins (replication protein A 8) supports the conclusion that correct refolding does occur. Based on these results, we discuss the refolding mechanism.",

keywords = "Denaturant, Detergent, Inclusion body, Polyethylene glycol, Refolding, Zeolite",

author = "Hiroyuki Chiku and Akiko Kawai and Toyotaka Ishibashi and Masahide Takehara and Takuro Yanai and Fujio Mizukami and Kengo Sakaguchi",

year = "2006",

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T1 - A novel protein refolding method using a zeolite

AU - Chiku, Hiroyuki

AU - Kawai, Akiko

AU - Ishibashi, Toyotaka

AU - Takehara, Masahide

AU - Yanai, Takuro

AU - Mizukami, Fujio

AU - Sakaguchi, Kengo

PY - 2006/1/15

Y1 - 2006/1/15

N2 - We have succeeded in developing a simple and effective protein refolding method using the inorganic catalyst, β-zeolite. The method involves the adsorption of proteins solubilized with 6 M guanidine hydrochroride from inclusion body (IB) preparations onto the zeolite. The denaturant is then removed, and the proteins in the IBs are released from the zeolite with polyoxyethylene detergent and salt. All of the IBs tested (11 different species) were successfully refolded under these conditions. The refolded proteins are biochemically active, and NMR analysis of one of the proteins (replication protein A 8) supports the conclusion that correct refolding does occur. Based on these results, we discuss the refolding mechanism.

AB - We have succeeded in developing a simple and effective protein refolding method using the inorganic catalyst, β-zeolite. The method involves the adsorption of proteins solubilized with 6 M guanidine hydrochroride from inclusion body (IB) preparations onto the zeolite. The denaturant is then removed, and the proteins in the IBs are released from the zeolite with polyoxyethylene detergent and salt. All of the IBs tested (11 different species) were successfully refolded under these conditions. The refolded proteins are biochemically active, and NMR analysis of one of the proteins (replication protein A 8) supports the conclusion that correct refolding does occur. Based on these results, we discuss the refolding mechanism.

KW - Denaturant

KW - Detergent

KW - Inclusion body

KW - Polyethylene glycol

KW - Refolding

KW - Zeolite

UR - https://www.webofscience.com/wos/woscc/full-record/WOS:000234635200015

UR - https://openalex.org/W2015192894

UR - https://www.scopus.com/pages/publications/29244459995

U2 - 10.1016/j.ab.2005.10.032

DO - 10.1016/j.ab.2005.10.032

M3 - Journal Article

C2 - 16316618

SN - 0003-2697

VL - 348

SP - 307

EP - 314

JO - Analytical Biochemistry

JF - Analytical Biochemistry

IS - 2

ER -

A novel protein refolding method using a zeolite

Abstract

Keywords

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