http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-H05161498-A
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_e45efeaa6a34dfd9d44fa29a7fe0c806 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-40 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P19-44 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07H15-203 |
| filingDate | 1991-12-10-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_aa09c05cfe155f8f7857883dd4924a9d http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_459cb636f17a504747b3d104167949c6 |
| publicationDate | 1993-06-29-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | JP-H05161498-A |
| titleOfInvention | Method for producing non-reducing end-modified phenylated maltotetraose derivative |
| abstract | (57) [Summary] [Structure] General formula useful as a substrate for measuring α-amylase activity In the production of the non-reducing end-modified phenylated maltotetraose derivative represented by (wherein each symbol is as defined in the specification), a glycosyl transfer reaction by cyclodextrin glucanotransferase is utilized. Method. [Effect] According to the method of the present invention, a non-reducing end-modified phenylated maltotetraose derivative useful as a substrate for measuring α-amylase activity can be efficiently synthesized by a sugar rearrangement reaction by cyclodextrin glucanotransferase. .. |
| isCitedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-S5890798-U |
| priorityDate | 1991-12-10-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 99.