Biocatalytic Preparation of N-Glycolylneuraminic Acid, Deaminoneuraminic Acid (KDN) and 9-Azido-9-deoxysialic Acid Oligosaccharides

2003 ◽  
Vol 345 (67) ◽  
pp. 687-690 ◽  
Author(s):  
Ola Blixt ◽  
James C. Paulson
Keyword(s):  
Deaminoneuraminic Acid

Ceruloplasmin carries the anionic glycan oligo/poly α2,8 deaminoneuraminic acid

2002 ◽  
Vol 295 (3) ◽  
pp. 597-602 ◽  
Author(s):  
Martin Ziak ◽  
Mirjam Meier ◽  
Ilse Novak-Hofer ◽  
Jürgen Roth
Keyword(s):  
Deaminoneuraminic Acid

scholarly journals Molecular cloning of a unique CMP-sialic acid synthetase that effectively utilizes both deaminoneuraminic acid (KDN) and N-acetylneuraminic acid (Neu5Ac) as substrates

Glycobiology ◽  
2001 ◽  
Vol 11 (8) ◽  
pp. 685-692 ◽  
Author(s):  
D. Nakata ◽  
A.-K. Munster ◽  
R. Gerardy-Schahn ◽  
N. Aoki ◽  
T. Matsuda ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Molecular Cloning ◽  
Acetylneuraminic Acid ◽  
Deaminoneuraminic Acid

scholarly journals Identification of Megalin as the Sole Rat Kidney Sialoglycoprotein Containing Poly α2,8 Deaminoneuraminic Acid

1999 ◽  
Vol 10 (2) ◽  
pp. 203-209
Author(s):  
MARTIN ZIAK ◽  
DONTSCHO KERJASCHKI ◽  
MARILYN G. FARQUHAR ◽  
JÜRGEN ROTH
Keyword(s):  
Rat Kidney ◽  
Ldl Receptor ◽  
Amino Acid Sequences ◽  
Purification And Characterization ◽  
Receptor Associated Protein ◽  
Mammalian Tissues ◽  
Convoluted Tubules ◽  
Receptor Family ◽  
Deaminoneuraminic Acid

Abstract. Recently, poly α2,8 deaminoneuraminic acid (poly α2,8 KDN) was demonstrated in various embryonic and adult mammalian tissues. This study reports the purification and characterization of the single poly α2,8 KDN-bearing glycoprotein from rat kidney. Amino acid sequences of proteolytic fragments shared homology with megalin, a member of the LDL receptor family. Immunochemical analysis supported this finding, since immunoprecipitated poly α2,8 KDN-bearing glycoprotein was immunoreactive with anti-megalin antibodies in Western blotting and conversely immunoprecipitated megalin was immunoreactive with the monoclonal anti-poly α2,8 KDN antibody. Furthermore, receptor-associated protein affinity-purified megalin reacted with the anti-poly α2,8 KDN antibody. By immunoelectron microscopy, labeling for both poly α2,8 KDN and megalin coincided in the brush border, endocytic invaginations and vesicles, and apical dense tubules of proximal convoluted tubules. Immunoreactivity for poly α2,8 KDN on purified megalin was abolished by β-elimination reaction but not by N-glycosidase F treatment. These data identified megalin as the sole glycoprotein of rat kidney, which contains poly α2,8 KDN present on O-glycosidically linked oligosaccharides. Furthermore, this study shows that megalin carries N-glycosidically linked hybrid and complex-type oligosaccharides terminating with sialic acid. Both poly α2,8 KDN and sialic acids on megalin may contribute to the binding of Ca2+ and cationic ligands.

Sign in / Sign up

Export Citation Format

Share Document