- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1007/s10930-004-1513-9
-
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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
- Language:
- English
- Keywords:
- Copyright date:
- 2005
Journal article
Over-expression, purification, and characterization of recombinant human arylamine N-acetyltransferase 1.
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