Glycosylation of endogenous protein(s) of the rough and smooth microsomes by a lipid sugar intermediate

Several problems regarding the protein acceptor of the oligosaccharide from GEA (glucosylated endogenous acceptor) were investigated in the present work using rat liver microsomal subfractions. It was found that the acceptor molecule is present in rough and smooth liver microsomes. Furthermore both...

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Autor principal:	Carminatti, Héctor
Publicado:	1977
Materias:	glucose lipid protein glycosylation in vitro study liver microsome rat theoretical study Animal Deoxycholic Acid Glycolipids Glycoproteins Kinetics Male Microsomes, Liver Oligosaccharides Puromycin Rats Ribosomes Support, U.S. Gov't, P.H.S.
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v16_n2-3_p171_IdoyagaVargas http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p171_IdoyagaVargas
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_03008177_v16_n2-3_p171_IdoyagaVargas
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spelling	paper:paper_03008177_v16_n2-3_p171_IdoyagaVargas2023-06-08T15:27:23Z Glycosylation of endogenous protein(s) of the rough and smooth microsomes by a lipid sugar intermediate Carminatti, Héctor glucose lipid protein glycosylation in vitro study liver microsome rat theoretical study Animal Deoxycholic Acid Glycolipids Glycoproteins Kinetics Male Microsomes, Liver Oligosaccharides Puromycin Rats Ribosomes Support, U.S. Gov't, P.H.S. Several problems regarding the protein acceptor of the oligosaccharide from GEA (glucosylated endogenous acceptor) were investigated in the present work using rat liver microsomal subfractions. It was found that the acceptor molecule is present in rough and smooth liver microsomes. Furthermore both fractions have closely similar specific activities. The problem of whether nascent peptides must be ribosome bound for glycosylation to occur was studied. The results suggests that binding of peptides to ribosomes is not a necessary condition for the transfer of GEA oligosaccharide to protein. The increase in specific activity found after partial release of the microsomal vesicular content suggests that the acceptor protein for GEA is membrane bound. Evidence obtained in attempting to elucidate whether nascent or completed chains are glycosylated favours the later possibility. © 1977 Dr. W. Junk b.v. Publishers. Fil:Carminatti, H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1977 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v16_n2-3_p171_IdoyagaVargas http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p171_IdoyagaVargas
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	glucose lipid protein glycosylation in vitro study liver microsome rat theoretical study Animal Deoxycholic Acid Glycolipids Glycoproteins Kinetics Male Microsomes, Liver Oligosaccharides Puromycin Rats Ribosomes Support, U.S. Gov't, P.H.S.
spellingShingle	glucose lipid protein glycosylation in vitro study liver microsome rat theoretical study Animal Deoxycholic Acid Glycolipids Glycoproteins Kinetics Male Microsomes, Liver Oligosaccharides Puromycin Rats Ribosomes Support, U.S. Gov't, P.H.S. Carminatti, Héctor Glycosylation of endogenous protein(s) of the rough and smooth microsomes by a lipid sugar intermediate
topic_facet	glucose lipid protein glycosylation in vitro study liver microsome rat theoretical study Animal Deoxycholic Acid Glycolipids Glycoproteins Kinetics Male Microsomes, Liver Oligosaccharides Puromycin Rats Ribosomes Support, U.S. Gov't, P.H.S.
description	Several problems regarding the protein acceptor of the oligosaccharide from GEA (glucosylated endogenous acceptor) were investigated in the present work using rat liver microsomal subfractions. It was found that the acceptor molecule is present in rough and smooth liver microsomes. Furthermore both fractions have closely similar specific activities. The problem of whether nascent peptides must be ribosome bound for glycosylation to occur was studied. The results suggests that binding of peptides to ribosomes is not a necessary condition for the transfer of GEA oligosaccharide to protein. The increase in specific activity found after partial release of the microsomal vesicular content suggests that the acceptor protein for GEA is membrane bound. Evidence obtained in attempting to elucidate whether nascent or completed chains are glycosylated favours the later possibility. © 1977 Dr. W. Junk b.v. Publishers.
author	Carminatti, Héctor
author_facet	Carminatti, Héctor
author_sort	Carminatti, Héctor
title	Glycosylation of endogenous protein(s) of the rough and smooth microsomes by a lipid sugar intermediate
title_short	Glycosylation of endogenous protein(s) of the rough and smooth microsomes by a lipid sugar intermediate
title_full	Glycosylation of endogenous protein(s) of the rough and smooth microsomes by a lipid sugar intermediate
title_fullStr	Glycosylation of endogenous protein(s) of the rough and smooth microsomes by a lipid sugar intermediate
title_full_unstemmed	Glycosylation of endogenous protein(s) of the rough and smooth microsomes by a lipid sugar intermediate
title_sort	glycosylation of endogenous protein(s) of the rough and smooth microsomes by a lipid sugar intermediate
publishDate	1977
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v16_n2-3_p171_IdoyagaVargas http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p171_IdoyagaVargas
work_keys_str_mv	AT carminattihector glycosylationofendogenousproteinsoftheroughandsmoothmicrosomesbyalipidsugarintermediate
_version_	1768542218850664448

Glycosylation of endogenous protein(s) of the rough and smooth microsomes by a lipid sugar intermediate

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