http://rdf.ncbi.nlm.nih.gov/pubchem/patent/FI-885464-A
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_d21cbff64022f95c237c0bd3ec8656ca |
| classificationCPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/Y02A50-30 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K39-02 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K39-0275 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-18 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P31-04 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P19-44 |
| classificationIPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-91 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61P31-04 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K39-395 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K39-39 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-18 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K39-02 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P19-44 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N- http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K38-46 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K39-00 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07H13-06 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K9-08 |
| filingDate | 1988-11-24-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_545910a8caee398349306ed4fa8b3f8f http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_b10985ff52f2adcd7de65931e0c74cd7 |
| publicationDate | 1988-11-24-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | FI-885464-A |
| titleOfInvention | Acyloxy acyl hydrolase and its use |
| abstract | An acyloxyacyl hydrolase from the human promyelocyte cell line HL-60 has been found to specifically hydrolyze fatty acids form their ester linkages to hydroxy groups of 3- hydroxyfatty acids, the latter being bound in turn to LPS glycosaminyl residues. The hydrolyzed fatty acids may include dodecanoic acid, tetradecanoic acid and hexadecanoic acid. This enzyme showed a molecular weight, between 50,000 and 70,000 daltons, measured cromatographically using gel filtration. Altered bacterial LPS substantially without fatty acids bound to hydroxyl group of 3-hydroxyfatty acids covalently linked to a glucosaminyl moiety of LPS lipid A are produced. Since the structure of the lipid A moiety is highly conserved, acyloxyacyl hydrolase may act on the LPS of many different pathogenic bacteria (for example Salmonella, Escherichia, Haemophilus, and Neisseria). Such altered bacterial LPS, having toxicity reduced more than immunostimulatory activity, may be therapeutically useful: 1 as vaccines to prevent gram-negative bacterial diseases by inducing antibodies to LPS 0-polysaccharide or R-core antigens, 2 as antidotes to treat or prevent gram-negative bacterial septicaemia ("septic shock"), or 3 as adjuvants to enhance formation of antibodies to other antigens. The acyloxyacyl hydrolase itself may be prophylactically or therapeutically useful to detoxify endogenous LPS in patients with gram-negative bacterial diseases. The enzyme may also be used to remove toxic LPS from therapeutic injectants. |
| priorityDate | 1986-05-28-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 42.