http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-5861296-A
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_d55dd4da0d8f5bfa72abe0507617311d |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-14 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-14 |
| filingDate | 1995-10-23-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 1999-01-19-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_a6d2e8701b1d09c368a918dbaa8419c6 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_27bf7121ffc73e42a8137e013c2a4b0b http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_769ef8ccc1298fe5869fd0e1ddba4f9a |
| publicationDate | 1999-01-19-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | US-5861296-A |
| titleOfInvention | Purified thermostable inorganic pyprophosphatase obtainable from thermococcus litoralis |
| abstract | PCT No. PCT/US95/13662 Sec. 371 Date Mar. 12, 1997 Sec. 102(e) Date Mar. 12, 1997 PCT Filed Oct. 23, 1995 PCT Pub. No. WO96/12798 PCT Pub. Date May 2, 1996The present invention provides an extremely thermostable enzyme obtainable from Thermococcus litoralis. The enzyme, in inorganic pyrophosphatase (sometimes referred to herein as "PPase"), catalyzes the hydrolysis of inorganic pyrophosphate (PPi) to form two molecules of orthophophate (Pi).P2O7-4+H2O->2HPO4-2The present invention also provides a purification process for obtaining the inorganic pyrophosphatase from Thermococcus litoralis. In addition, characterization of the enzyme reveals a multimeric enzyme (125 kDa) with six identical subunits of 20-21 kDa as revealed by SDS-PAGE. Moreover, the enzyme exhibits unusual stability and maintains 100% of its activity after being incubated at 100 DEG C. in the absence of Mg2+ for 4 hours. Furthermore, the complete amino acid and nucleic acid sequence has been obtained; the amino acid sequence shows similarity to known PPase sequences and likely functional residues appear to be conserved. The thermostable enzyme may be native or recombinant and may be used for DNA sequencing or DNA amplification to eliminate the problems of pyrophosphorolysis. |
| isCitedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/patent/WO-2004072230-A2 http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-2003162263-A1 http://rdf.ncbi.nlm.nih.gov/pubchem/patent/WO-2004072230-A3 http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-2004170981-A1 http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-113481180-A |
| priorityDate | 1994-10-25-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
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