http://rdf.ncbi.nlm.nih.gov/pubchem/patent/WO-0214471-A2
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_849b911cd7cbdf4376e75df5b8711342 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P9-00 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-501 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-50 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-70 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K38-00 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P21-02 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-50 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-09 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N7-01 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-73 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-70 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61P9-00 |
| filingDate | 2001-08-15-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_3692d56db4cf9eba87d4da8aa26c8641 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_3d789a23b377fae76a02b5d00723099f http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_34c7521e05d99b03ab510b444b49904a http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_c6c4996c6791ba7d8dab29fad7c5ffd1 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_df334a96255761f465de8f6e1bc62133 |
| publicationDate | 2002-02-21-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | WO-0214471-A2 |
| titleOfInvention | A method of producing biologically active human acidic fibroblast growth factor and its use in promoting angiogenesis |
| abstract | The gene of human acidic fibroblast growth factor 155 (haFGF 155) has been obtained by chemical synthesis. The nucleotide sequence of haFGF 155 gene has been deduced on the basis of haFGF 155 amino acid sequence as described in the literature. The amino acid sequence of the synthesized haFGF 155 does not differ from those described in the literature. The nucleotide sequence of haFGF gene differs from those described previously. For chemical synthesis of haFGF 155 gene, codons were used which are the ones most often used by E. coli in highly expressed E. coli proteins. A plasmid with haFGF 155 (phaFGF 155) gene was obtained and was used to transform E. coli. Production of haFGF 154 protein was achieved by cultivation of the producer strain under conditions which slow down the lytic development of lambda phage. The haFGF 154 protein accumulated in culture medium in a soluble condition as a result of the producer strain cells lysis by the lambda phage. The haFGF 154 protein constituted 20% of the soluble protein accumulated in the culture medium and its biological activity was demonstrated by its ability to generate new vessels (angiogenesis). The initiator methionine residue at position 1 of the FGF 155 protein was completely removed during protein synthesis resulting in an FGF 154 amino acid product. The use of the phage-dependent method to produce other forms of the haFGF protein is also disclosed. |
| isCitedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/patent/EA-009390-B1 http://rdf.ncbi.nlm.nih.gov/pubchem/patent/EP-2338909-A1 http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-7956033-B2 |
| priorityDate | 2000-08-15-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 356.