Expression, Refolding and Characterization of Human Brain Serine Racemase in Escherichia coli with N-Terminal His-Tag

Chizuru Nagayoshi; Matsujiro Ishibashi; Yoshiko Kita; Masaaki Matsuoka; Ikuo Nishimoto; Masao Tokunaga

doi:10.2174/0929866054395284

ISSN: 0929-8665
E-ISSN: 1875-5305

Expression, Refolding and Characterization of Human Brain Serine Racemase in Escherichia coli with N-Terminal His-Tag
Authors: Chizuru Nagayoshi¹, Matsujiro Ishibashi², Yoshiko Kita³, Masaaki Matsuoka⁴, Ikuo Nishimoto⁵ and Masao Tokunaga⁶
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¹ Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan. ² Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan. ³ Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan. ⁴ Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan. ⁵ Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan. ⁶ Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan.
Source: Protein and Peptide Letters, Volume 12, Issue 5, Jul 2005, p. 487 - 490
DOI: https://doi.org/10.2174/0929866054395284
- Available online: 01 Jul 2005

Abstract

Human brain serine racemase (hSR) was expressed in large amounts in E. coli with N-terminal His-tag (HishSR). His-hSR expressed in inclusion body was solubilized and purified to homogeneity by Ni-NTA affinity column. Purified His-hSR was refolded in Tween 20/cycloamylose with ∼50% efficiency, and refolded His-hSR was isolated by Q Sepharose column chromatography. The refolding conditions are described in detail. His-hSR catalyzed the elimination of L-Ser as well as L-Ser-O-sulfate to form pyruvate.

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2005-07-01

2025-10-21

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Article Type: Review Article

Keyword(s): cycloamylose; d-ser; detergents; human brain serine racemase; nmda receptor; refolding

Expression, Refolding and Characterization of Human Brain Serine Racemase in Escherichia coli with N-Terminal His-Tag

Abstract

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