Lectin affinity of Junin virus glycoproteins

We studied the binding of Junin virus (Arenaviridae) glycoproteins, G1 and G2, to two insolubilized lectins. The results showed that mannose, N-acetyl-glucosamine and galactose residues were exposed on G2, while only the latter predominated on G1. Heterogeneity of carbohydrate chains was found in G2...

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Publicado: 1988
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_07692617_v139_n_p277_Mersich
http://hdl.handle.net/20.500.12110/paper_07692617_v139_n_p277_Mersich
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spelling paper:paper_07692617_v139_n_p277_Mersich2025-07-30T18:22:14Z Lectin affinity of Junin virus glycoproteins Arenaviridae Chaîne des oligosides Glycoprotein Glycoprotéine Interactions Interactions Junin virus Lectin Lectine Oligosaccharide chains Virus Junín lectin virus glycoprotein arenavirus glycosylation immunoprecipitation junin virus nonhuman priority journal Animal Arenaviridae Arenaviruses, New World Chromatography, Affinity Lactoperoxidase Lectins Membrane Glycoproteins Support, Non-U.S. Gov't Vero Cells Viral Envelope Proteins We studied the binding of Junin virus (Arenaviridae) glycoproteins, G1 and G2, to two insolubilized lectins. The results showed that mannose, N-acetyl-glucosamine and galactose residues were exposed on G2, while only the latter predominated on G1. Heterogeneity of carbohydrate chains was found in G2, the only glycoprotein that was iodinated by the lactoperoxidase method. © 1988, Elsevier. All rights reserved. 1988 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_07692617_v139_n_p277_Mersich http://hdl.handle.net/20.500.12110/paper_07692617_v139_n_p277_Mersich
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Arenaviridae
Chaîne des oligosides
Glycoprotein
Glycoprotéine
Interactions
Interactions
Junin virus
Lectin
Lectine
Oligosaccharide chains
Virus Junín
lectin
virus glycoprotein
arenavirus
glycosylation
immunoprecipitation
junin virus
nonhuman
priority journal
Animal
Arenaviridae
Arenaviruses, New World
Chromatography, Affinity
Lactoperoxidase
Lectins
Membrane Glycoproteins
Support, Non-U.S. Gov't
Vero Cells
Viral Envelope Proteins
spellingShingle Arenaviridae
Chaîne des oligosides
Glycoprotein
Glycoprotéine
Interactions
Interactions
Junin virus
Lectin
Lectine
Oligosaccharide chains
Virus Junín
lectin
virus glycoprotein
arenavirus
glycosylation
immunoprecipitation
junin virus
nonhuman
priority journal
Animal
Arenaviridae
Arenaviruses, New World
Chromatography, Affinity
Lactoperoxidase
Lectins
Membrane Glycoproteins
Support, Non-U.S. Gov't
Vero Cells
Viral Envelope Proteins
Lectin affinity of Junin virus glycoproteins
topic_facet Arenaviridae
Chaîne des oligosides
Glycoprotein
Glycoprotéine
Interactions
Interactions
Junin virus
Lectin
Lectine
Oligosaccharide chains
Virus Junín
lectin
virus glycoprotein
arenavirus
glycosylation
immunoprecipitation
junin virus
nonhuman
priority journal
Animal
Arenaviridae
Arenaviruses, New World
Chromatography, Affinity
Lactoperoxidase
Lectins
Membrane Glycoproteins
Support, Non-U.S. Gov't
Vero Cells
Viral Envelope Proteins
description We studied the binding of Junin virus (Arenaviridae) glycoproteins, G1 and G2, to two insolubilized lectins. The results showed that mannose, N-acetyl-glucosamine and galactose residues were exposed on G2, while only the latter predominated on G1. Heterogeneity of carbohydrate chains was found in G2, the only glycoprotein that was iodinated by the lactoperoxidase method. © 1988, Elsevier. All rights reserved.
title Lectin affinity of Junin virus glycoproteins
title_short Lectin affinity of Junin virus glycoproteins
title_full Lectin affinity of Junin virus glycoproteins
title_fullStr Lectin affinity of Junin virus glycoproteins
title_full_unstemmed Lectin affinity of Junin virus glycoproteins
title_sort lectin affinity of junin virus glycoproteins
publishDate 1988
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_07692617_v139_n_p277_Mersich
http://hdl.handle.net/20.500.12110/paper_07692617_v139_n_p277_Mersich
_version_ 1840328632456708096