The specificity of viral and bacterial sialidases for α(2–3)- and α(2–6)-linked sialic acids in glycoproteins
Identifieur interne : 002573 ( Main/Exploration ); précédent : 002572; suivant : 002574The specificity of viral and bacterial sialidases for α(2–3)- and α(2–6)-linked sialic acids in glycoproteins
Auteurs : Anthony P. Corfield [Allemagne, Royaume-Uni] ; Herman Higa [États-Unis] ; James C. Paulson [États-Unis] ; Roland Schauer [Allemagne]Source :
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology [ 0167-4838 ] ; 1983.
English descriptors
- Teeft :
- Antifreeze, Antifreeze glycoprotein, Antifreeze glycoprotein substrates, Assay, Bacterial sialidases, Biol, Chem, Cholerae, Cholerae sialidase, Different glycosidic linkages, Glycoprotein, Glycoprotein substrates, Glycosidically, Linkage, Neu5ac, Neu5gc, Newcastle, Newcastle disease virus, Newcastle disease virus sialidase, Nmol, Oligosaccharide, Ovine submandibular gland glycoprotein, Paulson, Sialic, Sialic acid, Sialic acids, Sialidase, Sialidases, Sodium acetate, Ureafaciens, Ureafaciens sialidase, Viral, Viral sialidases.
Abstract
Abstract: The anomeric specificity of six sialidases (Vibrio cholerae, Arthrobacter ureafaciens, Clostridium perfringens, Newcastle disease virus, fowl plaque virus and influenza A2 virus sialidases) was assessed with sialylated antifreeze glycoprotein, ovine submandibular gland glycoprotein and α1-acid glycoprotein, resialylated specifically in α(2–3) or α(2–6) linkage with N-acetylneuraminic acid or N-glycolylneuraminic acid using highly purified sialyltransferases. The rate of release of sialic acid from these substrates was found to correlate well with the specificity observed earlier with the same sialidases using small oligosaccharide substrates, i.e., α(2–3) glycosidic linkages are hydrolyzed faster than α(2–6) linkages,w ith the exception of the enzyme from A. ureafaciens. Sialidase activity was higher with N-acetylneuraminic acid when compared with N-glycolylneuraminic acid. The studies also showed that the core oligosaccharide and protein structure in glycoproteins may influence the rate of release for different glycosidic linkages.
Url:
DOI: 10.1016/0167-4838(83)90080-8
Affiliations:
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Corfield</name><affiliation wicri:level="0"><country wicri:rule="zip">Allemagne</country></affiliation><affiliation wicri:level="1"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>∗Present address: Department of Medicine Laboratories, Bristol Royal Infirmary, University of Bristol, Bristol BS2 8HW</wicri:regionArea><wicri:noRegion>Bristol BS2 8HW</wicri:noRegion></affiliation></author><author><name sortKey="Higa, Herman" sort="Higa, Herman" uniqKey="Higa H" first="Herman" last="Higa">Herman Higa</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Department of Biological Chemistry, School of Medicine, University of California, Los Angeles</wicri:cityArea></affiliation></author><author><name sortKey="Paulson, James C" sort="Paulson, James C" uniqKey="Paulson J" first="James C." last="Paulson">James C. Paulson</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Department of Biological Chemistry, School of Medicine, University of California, Los Angeles</wicri:cityArea></affiliation></author><author><name sortKey="Schauer, Roland" sort="Schauer, Roland" uniqKey="Schauer R" first="Roland" last="Schauer">Roland Schauer</name><affiliation wicri:level="0"><country wicri:rule="zip">Allemagne</country></affiliation></author></analytic><monogr></monogr><series><title level="j">Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology</title><title level="j" type="abbrev">BBAPRO</title><idno type="ISSN">0167-4838</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1983">1983</date><biblScope unit="volume">744</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="121">121</biblScope><biblScope unit="page" to="126">126</biblScope></imprint><idno type="ISSN">0167-4838</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0167-4838</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Antifreeze</term><term>Antifreeze glycoprotein</term><term>Antifreeze glycoprotein substrates</term><term>Assay</term><term>Bacterial sialidases</term><term>Biol</term><term>Chem</term><term>Cholerae</term><term>Cholerae sialidase</term><term>Different glycosidic linkages</term><term>Glycoprotein</term><term>Glycoprotein substrates</term><term>Glycosidically</term><term>Linkage</term><term>Neu5ac</term><term>Neu5gc</term><term>Newcastle</term><term>Newcastle disease virus</term><term>Newcastle disease virus sialidase</term><term>Nmol</term><term>Oligosaccharide</term><term>Ovine submandibular gland glycoprotein</term><term>Paulson</term><term>Sialic</term><term>Sialic acid</term><term>Sialic acids</term><term>Sialidase</term><term>Sialidases</term><term>Sodium acetate</term><term>Ureafaciens</term><term>Ureafaciens sialidase</term><term>Viral</term><term>Viral sialidases</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The anomeric specificity of six sialidases (Vibrio cholerae, Arthrobacter ureafaciens, Clostridium perfringens, Newcastle disease virus, fowl plaque virus and influenza A2 virus sialidases) was assessed with sialylated antifreeze glycoprotein, ovine submandibular gland glycoprotein and α1-acid glycoprotein, resialylated specifically in α(2–3) or α(2–6) linkage with N-acetylneuraminic acid or N-glycolylneuraminic acid using highly purified sialyltransferases. The rate of release of sialic acid from these substrates was found to correlate well with the specificity observed earlier with the same sialidases using small oligosaccharide substrates, i.e., α(2–3) glycosidic linkages are hydrolyzed faster than α(2–6) linkages,w ith the exception of the enzyme from A. ureafaciens. Sialidase activity was higher with N-acetylneuraminic acid when compared with N-glycolylneuraminic acid. The studies also showed that the core oligosaccharide and protein structure in glycoproteins may influence the rate of release for different glycosidic linkages.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>Royaume-Uni</li><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><country name="Allemagne"><noRegion><name sortKey="Corfield, Anthony P" sort="Corfield, Anthony P" uniqKey="Corfield A" first="Anthony P." last="Corfield">Anthony P. Corfield</name></noRegion><name sortKey="Schauer, Roland" sort="Schauer, Roland" uniqKey="Schauer R" first="Roland" last="Schauer">Roland Schauer</name></country><country name="Royaume-Uni"><noRegion><name sortKey="Corfield, Anthony P" sort="Corfield, Anthony P" uniqKey="Corfield A" first="Anthony P." last="Corfield">Anthony P. Corfield</name></noRegion></country><country name="États-Unis"><region name="Californie"><name sortKey="Higa, Herman" sort="Higa, Herman" uniqKey="Higa H" first="Herman" last="Higa">Herman Higa</name></region><name sortKey="Paulson, James C" sort="Paulson, James C" uniqKey="Paulson J" first="James C." last="Paulson">James C. Paulson</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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