Article
Expression, purification, and characterization of recombinant S-adenosylhomocysteine hydrolase from the thermophilic archaeon Sulfolobus solfataricus.
Protein expression and purification - 1 Feb 2000
Porcelli M, Fusco S, Inizio T, Zappia V, Cacciapuoti G
Abstract excerpt
S-Adenosylhomocysteine hydrolase from Sulfolobus solfataricus was expressed in Escherichia coli by inserting the genomic fragment containing the gene encoding for S-adenosylhomocysteine hydrolase downstream the isopropyl-beta-d-thiogalactoside-inducible promoter of pTrc99A expression vector. An ATG positioned 25 bp upstream of the gene which is in frame with a stop codon was utilized as the initiation codon. This...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
