http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-2016041075-A

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assignee http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_5b65747ed78f05dd9ebe107b50ce2855
classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K1-04
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K1-22
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-09
filingDate 2015-11-19-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_ecf492b38a9327d999119998702b3c6e
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_adda1fc77edc2f9ca07351b81bacfc2b
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_9dbe5f856a0bb7787f8d7f2d513b2436
publicationDate 2016-03-31-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber JP-2016041075-A
titleOfInvention Modified biotin-binding protein
abstract Avidin or streptavidin and the like have extremely strong binding to biotin, so that the binding cannot be dissociated. Reversible binding is required for the purification of biotinylated biomolecules such as by affinity chromatography. Provision of a modified biotin-binding protein capable of reversible binding. [MEANS FOR SOLVING PROBLEMS] Mutation is introduced into wild-type tamavidin 2 with biotin-binding activity derived from the edible mushroom basidiomycete Tamogitake, by modifying the sequence of specific amino acids, thereby adjusting hydrogen bonding and binding biotin Then, a target modified biotin-binding protein having a biotin-binding ability that can be dissociated and having protease resistance was obtained. [Selection figure] None
priorityDate 2009-06-24-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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