Purification and characterization of a kanamycin nucleotidyltransferase from plasmid pUB110-carrying cells of Bacillus subtilis.
AUTOR(ES)
Sadaie, Y
RESUMO
The nucleotidyltransferase encoded by plasmid pUB110 was purified to greater than 95% purity with a 33% yield. The enzyme is a monomeric protein with a molecular weight of 34,000. The optimum pH for activity is 5, and the optimum MgCl2 concentration for activity is 18 mM. The enzyme, which is synthesized constitutively, is stable for several weeks at 4 degrees C. This enzyme would appear to be a good model gene product for the development of a pUB110 deoxyribonucleic acid-dependent in vitro protein-synthesizing system from Bacillus subtilis.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=293806Documentos Relacionados
- Functional analysis of the leading strand replication origin of plasmid pUB110 in Bacillus subtilis.
- Site-specific in vitro binding of plasmid pUB110 to Bacillus subtilis membrane fraction.
- A DNA sequence outside the pUB110 minimal replicon is required for normal replication in Bacillus subtilis.
- Molecular cloning of genetically active fragments of Bacillus DNA in Bacillus subtilis and properties of the vector plasmid pUB110.
- Replication origins of single-stranded-DNA plasmid pUB110.