Identification of oligo-N-glycolylneuraminic acid residues in mammal-derived glycoproteins by a newly developed immunochemical reagent and biochemical methods.

The Journal of Biological Chemistry
C SatoY Inoue

Abstract

The occurrence of the alpha2-->8-linked oligomeric form of N-glycolylneuraminic acid (oligo-Neu5Gc) residues in mammalian glycoproteins was unequivocally demonstrated using a newly developed anti-oligo/poly-Neu5Gc monoclonal antibody as well as by chemical and biochemical methods. First, the antibody, designated mAb.2-4B, which specifically recognized oligo/poly-Neu5Gc with a degree of polymerization of >2, was developed by establishing a hybridoma cell line from P3U1 myeloma cells fused with splenocytes from an MRL autoimmune mouse immunized with dipalmitoylphosphatidylethanolamine-conjugated oligo/poly-Neu5Gc. Second, oligo-Neu5Gc was shown to occur in glycoproteins derived from pig spleen by Western blot analysis using mAb.2-4B, which was also confirmed by fluorometric high performance liquid chromatographic analysis of the product of periodate oxidation/reduction/acid hydrolysis of the purified glycopeptide fractions and by TLC and 600-MHz 1H NMR spectroscopic analysis of their mild acid hydrolysates. Finally, the ubiquitous occurrence of oligo-Neu5Gc chains as glycoproteinaceous components in Wistar rat tissue was immunochemically indicated. This is the first example demonstrating the diversity in oligo/poly-Sia structure ...Continue Reading

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Citations

Nov 18, 1998·Current Opinion in Structural Biology·M MühlenhoffR Gerardy-Schahn
Jun 22, 2013·Journal of Biochemistry·Chihiro Sato, Ken Kitajima
Aug 6, 2005·Transplantation·Christopher BurlakMichael A Rees
Feb 11, 2003·The Journal of Biological Chemistry·Uichiro YabeKen Kitajima
May 26, 2018·Glycobiology·Xiaoqing ZhangXue-Long Sun
Jan 15, 1999·Analytical Biochemistry·C SatoK Kitajima

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