http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-H0851998-A

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assignee http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_382ccfc2ebebcaee15aa7cda4cee86bc
classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-48
filingDate 1994-08-10-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_f03c466fbe17c94e17bb98b31762af27
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_f376e69af363f50e8104734987e7939a
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_d9f4e9d3497e7e47309da608cf15120a
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_0b42859f03bc5b2b7d3d1c3df37f838a
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http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_f137029f448ce3e945fbc2f2b1c1cd7d
publicationDate 1996-02-27-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber JP-H0851998-A
titleOfInvention Glycosyltransferase activity assay
abstract (57) [Summary] [Constitution] The present invention provides a method for measuring the activity of a glycosyltransferase using a sugar donor and a sugar acceptor, wherein CMP- is used as the sugar donor. N-acetylneuraminic acid is used and N is used as a sugar acceptor. -The 6-position of the acetylglucosamine residue is inactivated 1 Α- (2 → 3) that binds sialic acid at the α- (2 → 3) position to the non-reducing end of galactose of type 1 sugar chain Provided is a method for measuring an activity of a glycosyltransferase, which comprises measuring a specific activity of a sialyltransferase. [Effect] According to the method of the present invention, α- contained in the sample It is possible to specifically measure the activity of α- (2 → 3) sialyltransferase with higher accuracy and sensitivity by excluding the influence of (2 → 6) sialyltransferase.
isCitedBy http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-2021085770-A1
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-2010285446-A
priorityDate 1994-08-10-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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