Pub. Date : 1992 Oct 5
PMID : 1400309
16 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | The enzymatic transfer of Gal in beta 1,3 linkage to the GalNAc moiety of the core structure R1-GlcNAc beta 1,6GalNAc alpha-O-R2. | cyclohexenoesculetin-beta-galactoside | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |
2 | The enzymatic transfer of Gal in beta 1,3 linkage to the GalNAc moiety of the core structure R1-GlcNAc beta 1,6GalNAc alpha-O-R2. | cyclohexenoesculetin-beta-galactoside | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |
3 | The enzymatic transfer of Gal in beta 1,3 linkage to the GalNAc moiety of the core structure R1-GlcNAc beta 1,6GalNAc alpha-O-R2. | N-acetylgalactosaminuronic acid | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |
4 | The enzymatic transfer of Gal in beta 1,3 linkage to the GalNAc moiety of the core structure R1-GlcNAc beta 1,6GalNAc alpha-O-R2. | N-acetylgalactosaminuronic acid | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |
5 | The enzymatic transfer of Gal in beta 1,3 linkage to the GalNAc moiety of the core structure R1-GlcNAc beta 1,6GalNAc alpha-O-R2. | 2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |
6 | The enzymatic transfer of Gal in beta 1,3 linkage to the GalNAc moiety of the core structure R1-GlcNAc beta 1,6GalNAc alpha-O-R2. | 2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |
7 | Synthetic glycosides containing the core, -Glc-NAc beta 1,6GalNAc alpha-, acted as acceptors for beta-galactosyltransferase of human ovarian tumor. | Glycosides | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |
8 | Synthetic glycosides containing the core, -Glc-NAc beta 1,6GalNAc alpha-, acted as acceptors for beta-galactosyltransferase of human ovarian tumor. | Glucose | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |
9 | The product from LGBn was isolated in microgram quantities and identified by fast atom bombardment mass spectrometry as LacNAc beta 1,6(Gal beta 1,3)GalNAc alpha-O-Bn. | N-acetyllactosamine | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |
10 | The product from LGBn was isolated in microgram quantities and identified by fast atom bombardment mass spectrometry as LacNAc beta 1,6(Gal beta 1,3)GalNAc alpha-O-Bn. | N-acetyllactosamine | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |
11 | The alpha GalNAc:beta 1,3Gal transferase was present in high concentration in ovarian tumor tissue (ovarian cancer serum----1.4; ascitic fluid----0.9; tumor----17.4). | N-acetylgalactosaminuronic acid | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |
12 | Fuc alpha 1,3GlcNAc beta 1,6GalNAc alpha-O-ONP had the highest affinity for the enzyme. | fuc alpha 1,3glcnac | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |
13 | Fuc alpha 1,3GlcNAc beta 1,6GalNAc alpha-O-ONP had the highest affinity for the enzyme. | alpha-o-onp | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |
14 | The present study demonstrates the feasibility of beta 1,3Gal attachment on alpha GalNAc, which has already been substituted by beta 1,6GlcNAc, then elongated by beta 1,4Gal and also terminated by alpha 1,3Fuc. | N-acetylgalactosaminuronic acid | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |
15 | The present study demonstrates the feasibility of beta 1,3Gal attachment on alpha GalNAc, which has already been substituted by beta 1,6GlcNAc, then elongated by beta 1,4Gal and also terminated by alpha 1,3Fuc. | N-acetylgalactosaminuronic acid | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |
16 | The present study demonstrates the feasibility of beta 1,3Gal attachment on alpha GalNAc, which has already been substituted by beta 1,6GlcNAc, then elongated by beta 1,4Gal and also terminated by alpha 1,3Fuc. | N-acetylgalactosaminuronic acid | UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 | Homo sapiens |