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Comparative cross-linking activities of lactose-specific plant and animal lectins and a natural lactose-binding immunoglobulin G fraction from human serum with asialofetuin

Comparative cross-linking activities of lactose-specific plant and animal lectins and a natural... Plant and animal lectins bind and cross-link certain multiantennary oligosaccharides, glycopeptides, and glycoproteins. This can lead to the formation of homogeneous cross-linked complexes, which may differ in their stoichiometry depending on the nature of the sugar receptor involved. As a precisely defined ligand, we have employed bovine asialofetuin (ASF), a glycoprotein that possesses three asparagine-linked triantennary complex carbohydrate chains with terminal LacNAc residues. In the present study, we have compared the carbohydrate cross-linking properties of two Lac-specific plant lectins, an animal lectin and a naturally occurring Lac-binding polyclonal iminunoglobulin G subfraction from human serum with the ligand. Quantitative precipitation studies of the Lac-specific plant lectins, Viscum album agglutinin and Ricinus communis agglutinin, and the Lac-specific 16 kDa dimenc galectin from chicken liver demonstrate that these lectins form specific, stoichiometric cross-linked complexes with ASF. At low concentrations of ASF, 1:9 ASF/lectin (monomer) complexes formed with both plant lectins and the chicken lectin. With increasing concentrations of ASF, 1:3 ASF/lectin (monomer) complexes formed with the lectins irrespective of their source or size. The naturally occurring polyclonal antibodies, however, revealed a different cross-linking behavior. They show the formation of 1:3 ASF/antibody (per Fab moiety) cross-linked complexes at all concentrations of ASF. These studies demonstrate that Lac-specific plant and animal lectins as well as the Lac-binding immunoglobulin subfraction form specific stoichiometric cross-linked complexes with ASF. These results are discussed in terms of the structure-function properties of multivalent lectins and antibodies. Key words asialofetuin Lac-specific lectins immunoglobulin subfraction © Oxford University Press « Previous | Next Article » Table of Contents This Article Glycobiology (1996) 6 (8): 843-849. doi: 10.1093/glycob/6.8.843 » Abstract Free Full Text (PDF) Free Classifications Original Article Services Article metrics Alert me when cited Alert me if corrected Find similar articles Similar articles in Web of Science Similar articles in PubMed Add to my archive Download citation Request Permissions Disclaimer Citing Articles Load citing article information Citing articles via CrossRef Citing articles via Scopus Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Gupta, D. Articles by Brewer, C. Search for related content PubMed PubMed citation Articles by Gupta, D. Articles by Kaltner, H. Articles by Dong, X. Articles by Gabius, H. J. Articles by Brewer, C. Related Content Load related web page information Share Email this article CiteULike Delicious Facebook Google+ Mendeley Twitter What's this? Search this journal: Advanced » Current Issue November 2015 25 (11) Alert me to new issues The Journal Submit now! About this journal Rights & Permissions Manuscript submission & review Dispatch date of the next issue This journal is a member of the Committee on Publication Ethics (COPE) We are mobile – find out more Journals Career Network Glycoscience resources Consortium for Functional Glycomics The Official Journal of The Society for Glycobiology Impact factor: 3.147 5-Yr impact factor: 3.212 Editor-in-Chief Robert S. Haltiwanger View full editorial board For Authors Instructions to authors Self-archiving policy Online submission Open access options for authors - visit Oxford Open This journal enables compliance with the NIH Public Access Policy Alerting Services Email table of contents Email Advance Access CiteTrack XML RSS feed Corporate Services Advertising sales Classified Advertising Reprints Supplements var taxonomies = ("SCI01000"); Most Most Read Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds A "Glyconutrient Sham" Formation of the glycan chains in the synthesis of bacterial peptidoglycan Fucose: biosynthesis and biological function in mammals Optimal and consistent protein glycosylation in mammalian cell culture » View all Most Read articles Most Cited Biological roles of oligosaccharides: all of the theories are correct Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites An evolving view of the eukaryotic oligosaccharyltransferase Evolutionary considerations in relating oligosaccharide diversity to biological function Glycosidases of the asparagine-linked oligosaccharide processing pathway » View all Most Cited articles Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department. 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Comparative cross-linking activities of lactose-specific plant and animal lectins and a natural lactose-binding immunoglobulin G fraction from human serum with asialofetuin

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Publisher
Oxford University Press
Copyright
Copyright © 2015 Oxford University Press
ISSN
0959-6658
eISSN
1460-2423
DOI
10.1093/glycob/6.8.843
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Abstract

Plant and animal lectins bind and cross-link certain multiantennary oligosaccharides, glycopeptides, and glycoproteins. This can lead to the formation of homogeneous cross-linked complexes, which may differ in their stoichiometry depending on the nature of the sugar receptor involved. As a precisely defined ligand, we have employed bovine asialofetuin (ASF), a glycoprotein that possesses three asparagine-linked triantennary complex carbohydrate chains with terminal LacNAc residues. In the present study, we have compared the carbohydrate cross-linking properties of two Lac-specific plant lectins, an animal lectin and a naturally occurring Lac-binding polyclonal iminunoglobulin G subfraction from human serum with the ligand. Quantitative precipitation studies of the Lac-specific plant lectins, Viscum album agglutinin and Ricinus communis agglutinin, and the Lac-specific 16 kDa dimenc galectin from chicken liver demonstrate that these lectins form specific, stoichiometric cross-linked complexes with ASF. At low concentrations of ASF, 1:9 ASF/lectin (monomer) complexes formed with both plant lectins and the chicken lectin. With increasing concentrations of ASF, 1:3 ASF/lectin (monomer) complexes formed with the lectins irrespective of their source or size. The naturally occurring polyclonal antibodies, however, revealed a different cross-linking behavior. They show the formation of 1:3 ASF/antibody (per Fab moiety) cross-linked complexes at all concentrations of ASF. These studies demonstrate that Lac-specific plant and animal lectins as well as the Lac-binding immunoglobulin subfraction form specific stoichiometric cross-linked complexes with ASF. These results are discussed in terms of the structure-function properties of multivalent lectins and antibodies. Key words asialofetuin Lac-specific lectins immunoglobulin subfraction © Oxford University Press « Previous | Next Article » Table of Contents This Article Glycobiology (1996) 6 (8): 843-849. doi: 10.1093/glycob/6.8.843 » Abstract Free Full Text (PDF) Free Classifications Original Article Services Article metrics Alert me when cited Alert me if corrected Find similar articles Similar articles in Web of Science Similar articles in PubMed Add to my archive Download citation Request Permissions Disclaimer Citing Articles Load citing article information Citing articles via CrossRef Citing articles via Scopus Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Gupta, D. Articles by Brewer, C. Search for related content PubMed PubMed citation Articles by Gupta, D. Articles by Kaltner, H. Articles by Dong, X. Articles by Gabius, H. J. Articles by Brewer, C. Related Content Load related web page information Share Email this article CiteULike Delicious Facebook Google+ Mendeley Twitter What's this? Search this journal: Advanced » Current Issue November 2015 25 (11) Alert me to new issues The Journal Submit now! About this journal Rights & Permissions Manuscript submission & review Dispatch date of the next issue This journal is a member of the Committee on Publication Ethics (COPE) We are mobile – find out more Journals Career Network Glycoscience resources Consortium for Functional Glycomics The Official Journal of The Society for Glycobiology Impact factor: 3.147 5-Yr impact factor: 3.212 Editor-in-Chief Robert S. Haltiwanger View full editorial board For Authors Instructions to authors Self-archiving policy Online submission Open access options for authors - visit Oxford Open This journal enables compliance with the NIH Public Access Policy Alerting Services Email table of contents Email Advance Access CiteTrack XML RSS feed Corporate Services Advertising sales Classified Advertising Reprints Supplements var taxonomies = ("SCI01000"); Most Most Read Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds A "Glyconutrient Sham" Formation of the glycan chains in the synthesis of bacterial peptidoglycan Fucose: biosynthesis and biological function in mammals Optimal and consistent protein glycosylation in mammalian cell culture » View all Most Read articles Most Cited Biological roles of oligosaccharides: all of the theories are correct Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites An evolving view of the eukaryotic oligosaccharyltransferase Evolutionary considerations in relating oligosaccharide diversity to biological function Glycosidases of the asparagine-linked oligosaccharide processing pathway » View all Most Cited articles Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department. Online ISSN 1460-2423 - Print ISSN 0959-6658 Copyright © 2015 Oxford University Press Oxford Journals Oxford University Press Site Map Privacy Policy Cookie Policy Legal Notices Frequently Asked Questions Other Oxford University Press sites: Oxford University Press Oxford Journals China Oxford Journals Japan Academic & Professional books Children's & Schools Books Dictionaries & Reference Dictionary of National Biography Digital Reference English Language Teaching Higher Education Textbooks International Education Unit Law Medicine Music Online Products & Publishing Oxford Bibliographies Online Oxford Dictionaries Online Oxford English Dictionary Oxford Language Dictionaries Online Oxford Scholarship Online Reference Rights and Permissions Resources for Retailers & Wholesalers Resources for the Healthcare Industry Very Short Introductions World's Classics function fnc_onDomLoaded() { var query_context = getQueryContext(); PF_initOIUnderbar(query_context,":QS:default","","JRN"); PF_insertOIUnderbar(0); }; if (window.addEventListener) { window.addEventListener('load', fnc_onDomLoaded, false); } else if (window.attachEvent) { window.attachEvent('onload', fnc_onDomLoaded); } var gaJsHost = (("https:" == document.location.protocol) ? "https://ssl." : "http://www."); document.write(unescape("%3Cscript src='" + gaJsHost + "google-analytics.com/ga.js' type='text/javascript'%3E%3C/script%3E")); try { var pageTracker = _gat._getTracker("UA-189672-16"); pageTracker._setDomainName(".oxfordjournals.org"); pageTracker._trackPageview(); } catch(err) {}

Journal

Glycobiology – Oxford University Press

Published: Dec 1, 1996

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