Nondenaturing solubilization of β2 microglobulin from inclusion bodies by L-arginine

被引:50
作者
Umetsu, M
Tsumoto, K
Nitta, S
Adschiri, T
Ejima, D
Arakawa, T
Kumagai, I
机构
[1] Tohoku Univ, Dept Biomol Engn, Grad Sch Engn, Aoba Ku, Sendai, Miyagi 9808579, Japan
[2] Tohoku Univ, Inst Multidisciplinary Res Adv Mat, Aoba Ku, Sendai, Miyagi 9808577, Japan
[3] Ajinomoto Co Inc, AminoSci Labs, Kawasaki, Kanagawa 2108681, Japan
[4] Alliance Prot Labs Inc, Thousand Oaks, CA 91360 USA
关键词
inclusion body; nondenaturing reagent; oligomerization; solubilizing reagent; spectroscopic analysis;
D O I
10.1016/j.bbrc.2004.12.156
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Expression of beta2 microglobulin (beta2m) in Escherichia coli resulted in formation of inclusion bodies. Attenuated total reflectance Fourier transform infrared analysis suggested a native-like secondary structure of beta2m in the inclusion bodies. Nondenaturing solubilization of the native-like beta2m from inclusion bodies was achieved Using L-arginine solution, which enables all efficient recovery of beta2m with little aggregation. Greater beta2m solubilization from inclusion bodies was obtained at higher temperatures. Low-temperature solubilization yielded beta2m with fluorescence properties identical to those of native beta2m, but its secondary structure was slightly normative. Solubilization at moderate temperature gave beta2m with an apparently native structure. We propose ail efficient nondenaturing solubilization method combining L-arginine and moderate temperature. (C) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码:189 / 197
页数:9
相关论文
共 37 条
[1]   Investigation of refolding condition for Pseudomonas fluorescens lipase by response surface methodology [J].
Ahn, JH ;
Lee, YP ;
Rhee, JS .
JOURNAL OF BIOTECHNOLOGY, 1997, 54 (03) :151-160
[2]   Oxidative refolding chromatography:: folding of the scorpion toxin Cn5 [J].
Altamirano, MM ;
García, C ;
Possani, LD ;
Fersht, AR .
NATURE BIOTECHNOLOGY, 1999, 17 (02) :187-191
[3]   PURIFICATION AND CHARACTERIZATION OF RECOMBINANT HUMAN P50(CSK) PROTEIN-TYROSINE KINASE FROM AN ESCHERICHIA-COLI EXPRESSION SYSTEM OVERPRODUCING THE BACTERIAL CHAPERONES GROES AND GROEL [J].
AMREIN, KE ;
TAKACS, B ;
STIEGER, M ;
MOLNOS, J ;
FLINT, NA ;
BURN, P .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (04) :1048-1052
[4]   The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation [J].
Arakawa, T ;
Tsumoto, K .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2003, 304 (01) :148-152
[5]   RENATURATION, PURIFICATION AND CHARACTERIZATION OF RECOMBINANT FAB-FRAGMENTS PRODUCED IN ESCHERICHIA-COLI [J].
BUCHNER, J ;
RUDOLPH, R .
BIO-TECHNOLOGY, 1991, 9 (02) :157-162
[6]   Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: Application of a novel protein folding screen [J].
Chen, GQ ;
Gouaux, E .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (25) :13431-13436
[7]   Structural proteomics: prospects for high throughput sample preparation [J].
Christendat, D ;
Yee, A ;
Dharamsi, A ;
Kluger, Y ;
Gerstein, M ;
Arrowsmith, CH ;
Edwards, AM .
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 2000, 73 (05) :339-345
[8]  
Clark EDB, 1998, CURR OPIN BIOTECH, V9, P157
[9]   Protein aggregation: folding aggregates, inclusion bodies and amyloid [J].
Fink, AL .
FOLDING & DESIGN, 1998, 3 (01) :R9-R23
[10]   Archaeal genomics [J].
Gaasterland, T .
CURRENT OPINION IN MICROBIOLOGY, 1999, 2 (05) :542-547