Improved recovery of active GST-fusion proteins from insoluble aggregates: solubilization and purification conditions using PKM2 and HtrA2 as model proteins-Reference-Cited by-同舟云学术

Improved recovery of active GST-fusion proteins from insoluble aggregates: solubilization and purification conditions using PKM2 and HtrA2 as model proteins

Published:2011-04-30 Issue:4 Volume:44 Page:279-284
ISSN:1976-6696
Container-title:BMB Reports
language:en
Short-container-title:BMB Reports

Author:

Park Dae-Wook,Kim Sang-Soo,Nam Min-Kyung,Kim Goo-Young,Kim Jung-Ho,Rhim Hyang-Shuk

Publisher

Korean Society for Biochemistry and Molecular Biology - BMB Reports

Subject

Molecular Biology,Biochemistry,General Medicine

Link

http://ocean.kisti.re.kr/downfile/crosscheck/ksbmb/JAKO201115037885213.pdf

Reference28 articles.

1. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase

2. Purification of Proteins Fused to Glutathione S-Transferase

3. Mr 26,000 antigen of Schistosoma japonicum recognized by resistant WEHI 129/J mice is a parasite glutathione S-transferase.

4. The serine protease HtrA2/Omi cleaves Parkin and irreversibly inactivates its E3 ubiquitin ligase activity

5. Autocatalytic Processing of HtrA2/Omi Is Essential for Induction of Caspase-dependent Cell Death through Antagonizing XIAP

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