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  A universal expression-purification system based on the coiled-coil interaction of myosin heavy chain

Wolber, V., Maeda, K., Schumann, R., Brandmeier, B., Wiesmüller, L., & Wittinghofer, A. (1992). A universal expression-purification system based on the coiled-coil interaction of myosin heavy chain. Nature Biotechnology, 10, 900-904. doi:10.1038/nbt0892-900.

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NatBiotechnol_10_1992_900.pdf (Any fulltext), 677KB
 
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 Creators:
Wolber, Vera1, Author              
Maeda, Kayo, Author
Schumann, Renate1, 2, Author              
Brandmeier, Birgit, Author
Wiesmüller, Lisa1, Author              
Wittinghofer, Alfred1, Author              
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1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Dietmar Manstein Group, Max Planck Institute for Medical Research, Max Planck Society, ou_1497708              

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 Abstract: We have constructed a series of Escherichia coli expression vectors that produce high yields of fusion proteins containing the C-terminal fragment of light meromyosin (LMM) from rabbit fast skeletal muscle. The fusion proteins retain the ability of LMM to form polymers in low salt and to be soluble in high salt. Thus they can be easily purified from bacterial extracts with a high salt-low salt extraction procedure and still retain their biochemical properties. We demonstrate the utility of this system for the heterologous production and simple purification of LMM fusions of p21H-ras, the neurofibromatosis type I protein and the Tat and protease proteins of HIV-1.

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Language(s): eng - English
 Dates: 1992-08-01
 Publication Status: Published in print
 Pages: 5
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 Table of Contents: -
 Rev. Type: Peer
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Title: Nature Biotechnology
Source Genre: Journal
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Publ. Info: New York : Gale Group Inc.
Pages: - Volume / Issue: 10 Sequence Number: - Start / End Page: 900 - 904 Identifier: ISSN: 1087-0156
CoNE: https://pure.mpg.de/cone/journals/resource/954926980065