pharmaceutical compositions of the superoxiddismutase bacillus and bacillus caldotenax contain stearothermophilus

摘要

The genes (sod) encoding Bacillus stearothermophilus and Bacillus caldotenax Mn-superoxide dismutase have been cloned in Escherichia coli and their entire nucleotide sequences determined. With the exception of the post-translationally cleaved N-terminal methionine residue, the predicted amino acid sequence of the B. stearothermophilus enzyme (BSMnSOD) exhibits 100 % similarity to the previously determined amino acid sequence. The B. caldoenax enzyme (BCMnSOD) differs by two amino acids from BSMnSOD. Both recombinant MnSOD's were shown to be functionally active in E. coli, both in vitro and in vivo, and were expressed to 47 % of the cells soluble protein by coupling their transcription to the E. coli trp promoter. The pharmaceutical use of these bacterial superoxide dismutases is described.