A Disulfide-bonded Dimer of the Golgi β-Galactoside α2,6-Sialyltransferase Is Catalytically Inactive yet Still Retains the Ability to Bind Galactose
Open Access
- 1 March 1996
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 271 (13) , 7758-7766
- https://doi.org/10.1074/jbc.271.13.7758
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- A chaperone with a sweet toothCurrent Biology, 1993
- The role of the carbohydrate chains of Galβ-1,4-GlcNAcα2,6-sialyltransferase for enzyme eactivityBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1993
- Kin recognitionFEBS Letters, 1993
- Targeting and retention of Golgi membrane proteinsCurrent Opinion in Cell Biology, 1993
- Target sizes of galactosyltransferase, sialyltransferase, and uridine diphosphatase in Golgi apparatus of rat liverBiochemistry, 1993
- Biosynthesis and intracellular transport of α‐2,6‐sialyltransferase in rat hepatoma cellsEuropean Journal of Biochemistry, 1992
- Purification, properties and cation activation of galactosyltransferase from lactating‐rat mammary Golgi membranesEuropean Journal of Biochemistry, 1988
- Subcellular organization of glycosylation in mammalian cellsBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1987
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Purification and Properties of Neuraminidase from Vibrio choleraeJournal of General Microbiology, 1961