http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-102250852-B

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assignee http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_481e47a46b1888cc0534cec84520655f
classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-10
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N5-10
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K39-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61P35-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21
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http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-54
filingDate 2011-06-11-04:00^^<http://www.w3.org/2001/XMLSchema#date>
grantDate 2013-06-12-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_daa06047ce2b17693197a96647321bfe
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_12fc1582c5f2b9ce5efcc3b8568d4b41
publicationDate 2013-06-12-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber CN-102250852-B
titleOfInvention Clone and expression of bovine recombinant alpha-1,3-galactoside transferase (GT)
abstract The invention relates to a recombinant zymoprotein having high activity and specific GT. According to the invention, the 80th to 368th amino acids of Inner Mongolia cow thymus GT proteins, the smallest water-soluble part with activity of GT, are employed. To further improve water-solubility and enzyme reaction activity of recombinant GT, through molecular designing and gene engineering reconstruction of natural proteins, the 160th amino acid of GT proline is modified to be lysine, the 241st amino acid of GT glutamic acid is modified to be glutamine, and therefore, recombinant zymoprotein with stronger enzymatic activity is obtained; the obtained recombinant zymoprotein has enzymatic activity 8 to 10 times that of existing zymoprotein and is applicable to the medical field of tumor treatment.
priorityDate 2011-06-11-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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