Expression, Purification, and Spectral Characterization of Phytochromes.

Difference spectrum Phytochromes Pichia pastoris Recombinant protein Streptavidin affinity chromatography

Journal

Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969

Informations de publication

Date de publication:
2019
Historique:
entrez: 19 7 2019
pubmed: 19 7 2019
medline: 31 3 2020
Statut: ppublish

Résumé

Expression and purification of recombinant proteins are important for the structure-function study of phytochromes. However, it is difficult to purify phytochrome proteins from natural sources or using a bacterial expression system, due to the presence of multiple phytochrome species and low expression and solubility, respectively. Here we describe the expression of recombinant full-length plant phytochromes in the yeast Pichia pastoris, and the spectral analysis of chromophore-assembled phytochromes before and after the purification by streptavidin affinity chromatography.

Identifiants

pubmed: 31317405
doi: 10.1007/978-1-4939-9612-4_7
doi:

Substances chimiques

Recombinant Proteins 0
Phytochrome 11121-56-5

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

95-111

Références

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Auteurs

Yun-Jeong Han (YJ)

Department of Biotechnology and Kumho Life Science Laboratory, Chonnam National University, Gwangju, Republic of Korea.

Jae-Yong Cho (JY)

Department of Biotechnology and Kumho Life Science Laboratory, Chonnam National University, Gwangju, Republic of Korea.

Jeong-Il Kim (JI)

Department of Biotechnology and Kumho Life Science Laboratory, Chonnam National University, Gwangju, Republic of Korea. kimji@jnu.ac.kr.

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Classifications MeSH