Bovine mammary gland UDP-GalNAc:GlcNAc-R 1→4- N -acetylgalactosaminyltransferase is glycoprotein hormone nonspecific and shows interaction with α-lactalbumin

Author： van den Nieuwenhof I.M.   Schiphorst W.E.C.M.   van Die I.   van den Eijnden D.H.  

Publisher： Oxford University Press

ISSN： 1460-2423

Source： Glycobiology, Vol.9, Iss.2, 1999-02, pp. : 115-123

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

Previous Menu Next

Abstract

Related content

Identification and characterization of a novel UDP-GalNAc:GlcA-R α1,4- N -acetylgalactosaminyltransferase from a human sarcoma cell line

By Goto F.  

Glycobiology, Vol. 9, Iss. 7, 1999-07 ,pp. : 697-703

Oxford University Press

Access to resources Recommend Favorite

Characterization of mammalian UDP-GalNAc:glucuronide α1-4- N -acetylgalactosaminyltransferase

By Manzi A.  

Glycobiology, Vol. 9, Iss. 10, 1999-10 ,pp. : 1053-1060

Oxford University Press

Access to resources Recommend Favorite

Purification and cDNA cloning of UDP-GlcNAc:GlcNAc1-3Gal1-4Glc(NAc)-R [GlcNAc to Gal]1,6 N -acetylglucosaminyltransferase from rat small intestine: a major carrier of dIGnT activity in rat small intestine

By Renkonen O.  

Glycobiology, Vol. 13, Iss. 5, 2003-05 ,pp. : 387-400

Oxford University Press

Access to resources Recommend Favorite

A Scintillation Proximity Assay for UDP-GalNAc:Polypeptide, N -Acetylgalactosaminyltransferase

By Baker C.A.   Poorman R.A.   Kezdy F.J.   Staples D.J.   Smith C.W.   Elhammer A.P.  

Analytical Biochemistry, Vol. 239, Iss. 1, 1996-07 ,pp. : 20-24

Elsevier

Access to resources Recommend Favorite

UDP-Gal: GlcNAc-R β1,4-galactosyltransferase—a target enzyme for drug design. Acceptor specificity and inhibition of the enzyme

By Brockhausen Inka   Benn Melinda   Bhat Shridhar   Marone Sandra   Riley John   Montoya-Peleaz Pedro   Vlahakis Jason   Paulsen Hans   Schutzbach John   Szarek Walter  

Glycoconjugate Journal, Vol. 23, Iss. 7-8, 2006-11 ,pp. : 525-541

Springer Publishing Company

Access to resources Recommend Favorite