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Journal article

Over-expression, purification, and characterization of recombinant human arylamine N-acetyltransferase 1.

Abstract:

Human arylamine N-acetyltransferase 1 (NAT1) has been overexpressed in E. coli as a mutant dihydrofolic acid reductase (DHFR) fusion protein with a thrombin sensitive linker. An initial DEAE anion-exchange chromatography resulted in partial purification of the fusion protein. The fusion protein was cleaved with thrombin, and human rNAT1 was purified with a second DEAE column. A total of 8 mg of human rNAT1 from 2 1 of cell culture was purified to homogeneity with this methodology. Arylamine s...

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Publication status:
Published

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Publisher copy:
10.1007/s10930-004-1513-9

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry, BHF Centre of Research Excellence
Role:
Author
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Journal:
The protein journal
Volume:
24
Issue:
2
Pages:
65-77
Publication date:
2005-02-05
DOI:
EISSN:
1875-8355
ISSN:
1572-3887
URN:
uuid:251a9732-dfad-449c-96c4-d5589bf7b016
Source identifiers:
281493
Local pid:
pubs:281493

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