Two Naturally Occurring α2,6-Sialyltransferase Forms with a Single Amino Acid Change in the Catalytic Domain Differ in Their Catalytic Activity and Proteolytic Processing
Open Access
- 1 January 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (1) , 672-679
- https://doi.org/10.1074/jbc.272.1.672
Abstract
No abstract availableKeywords
This publication has 71 references indexed in Scilit:
- The Sialoadhesins ? A family of sialic acid-dependent cellular recognition molecules within the immunoglobulin superfamilyGlycoconjugate Journal, 1996
- Characterization of Terminal Sialic Acid Linkages on Human ThymocytesJournal of Biological Chemistry, 1996
- A Disulfide-bonded Dimer of the Golgi β-Galactoside α2,6-Sialyltransferase Is Catalytically Inactive yet Still Retains the Ability to Bind GalactoseJournal of Biological Chemistry, 1996
- Leukocyte Trafficking Mediated by Selectin-Carbohydrate InteractionsJournal of Biological Chemistry, 1995
- Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamilyCurrent Biology, 1994
- Biological roles of oligosaccharides: all of the theories are correctGlycobiology, 1993
- Polysialylation: from bacteria to brainsGlycobiology, 1992
- Tissue-specific Expression of β-Galactoside α-2,6-SialyltransferasePublished by Elsevier ,1989
- Tumor-Associated Carbohydrate AntigensAnnual Review of Immunology, 1984
- Carbohydrate-Specific Receptors of the LiverAnnual Review of Biochemistry, 1982