| Predicate |
Object |
| classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K38-00 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P9-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-0089
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-71 |
| classificationIPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K38-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-07
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-19 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-71
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61P9-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K38-44
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-02
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-53
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-09 |
| filingDate |
1991-08-02-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate |
2002-12-10-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_5d414caaaf4345c2b0e3cda30e6682a1
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_5d48272ac0c1e3fa74f81ccbb069cd9c
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_4b7855c7ed35d3f31d75bdead1f26ea6
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_63af3dd6de7426aca89bc1a41f18a514
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_bb9054449bcb3b0f5b7194dc5945d26b |
| publicationDate |
2002-12-10-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
CA-2088574-C |
| titleOfInvention |
Process for producing enzymes having superoxide dismutase activity, novel superoxide dismutase enzymes and novel pharmaceutical compositions comprising enzymes having superoxide dismutase activity |
| abstract |
The genes (sod) encoding Bacillus stearothermophi-lus 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. stearothermophi-lus enzyme (BSMnSOD) exhibits 100 % similarity to the previously determined amino acid sequence. The B, caldoe-nax 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 coup-ling their transcription to the E. coli trp promoter. The pharmaceutical use of these bacterial superoxide dismu-tases is described. |
| priorityDate |
1990-08-03-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |