Over-expression, purification, and characterization of recombinant human arylamine N-acetyltransferase 1.
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...
Principais autores: | Wang, H, Vath, G, Kawamura, A, Bates, C, Sim, E, Hanna, P, Wagner, C |
---|---|
Formato: | Journal article |
Idioma: | English |
Publicado em: |
2005
|
Registros relacionados
-
Eukaryotic arylamine N-acetyltransferase. Investigation of substrate specificity by high-throughput screening.
por: Kawamura, A, et al.
Publicado em: (2005) -
Neuroendocrine expression of mouse arylamine N-acetyltransferase 2
por: Wakefield, L, et al.
Publicado em: (2006) -
Structure and mechanism of arylamine N-acetyltransferases.
por: Westwood, I, et al.
Publicado em: (2006) -
Arylamine N-acetyltransferase in adult mouse brain
por: Mo, M, et al.
Publicado em: (2004) -
Hamster arylamine N-acetyltransferase 2: Investigation of substrate specificity by high-through-put screening
por: Kawamura, A, et al.
Publicado em: (2004)