Purification and functional reconstitution of the human Wilson copper ATPase, ATP7B.
- Portmann R Department of Clinical Pharmacology, University of Berne, Murtenstrasse 35, 3010 Berne, Switzerland.
- Solioz M
- 2005-06-21
Published in:
- FEBS letters. - 2005
Adenosine Triphosphatases
Cation Transport Proteins
Copper
Copper-Transporting ATPases
Hepatolenticular Degeneration
Humans
Saccharomyces cerevisiae
English
Wilson disease is a disorder of copper metabolism, due to inherited mutations in the Wilson copper ATPase gene ATP7B. To purify and study the function of the ATPase, the enzyme was truncated by five of the six metal binding domains and endowed with an N-terminal histidine-tag for affinity purification. This construct, delta1-5WNDP, was able to functionally complement a yeast strain defective in its native copper ATPase CCC2. Delta1-5WNDP was purified by Ni-affinity chromatography and reconstituted into proteoliposomes. This allowed, for the first time, the functional study of the Wilson ATPase in a purified, reconstituted system.
- Language
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- English
- Open access status
- bronze
- Identifiers
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- DOI 10.1016/j.febslet.2005.05.042
- PMID 15963506
- Persistent URL
- https://sonar.ch/global/documents/1072
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