http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-3015886-B1
Outgoing Links
Predicate | Object |
---|---|
classificationCPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/Y10S435-814 |
classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Q1-37 |
classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-37 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-09 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N21-64 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/G01N21-78 |
filingDate | 1998-11-04-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
grantDate | 2000-03-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationDate | 2000-03-06-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationNumber | JP-3015886-B1 |
titleOfInvention | A rapid method for the determination of asparagine residue-specific endoprotease activity from plants |
abstract | Abstract: PROBLEM TO BE SOLVED: To provide a method for quantifying an enzyme activity of a plant-derived asparagine residue-specific endoprotease, which can be measured quickly and more specifically and easily. thing. An oligopeptide having at least one asparagine residue in an amino acid sequence and having a C-terminal side of the asparagine residue other than any of an isoleucine residue, a leucine residue and a valine residue, comprising: Coumarin-4-yl-acetyl group on the N-terminal side, A plant characterized in that the fluorescence generated from a quenching fluorescent substrate cleaved by an asparagine residue-specific endoprotease is measured using a quenching fluorescent substrate having a 2,4-dinitrophenyl group disposed on the C-terminal side. Rapid method for quantifying asparagine residue-specific endoprotease activity. |
isCitedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/patent/WO-0109165-A3 |
priorityDate | 1998-11-04-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 92.