Oligosaccharide transfer from lipid sugar intermediates to endogenous protein(s) of rat liver microsomal subfractions

The subcellular localization and characterization of some of the components involved in the glycosylation of asparagine type glycoproteins was attempted using dolichyl diphosphate [14c]mannose oligosaccharide as precursor of the glycosylation reaction in vitro. Isolated rough and smooth microsomel f...

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Autores principales:	Burrone, Oscar R., Carminatti, Héctor
Publicado:	1979
Materias:	drug derivative glycoprotein isoprenoid phosphate sugar mannose membrane protein animal article biosynthesis enzymology intracellular membrane liver microsome metabolism polysome rat Animal Glycoproteins Intracellular Membranes Mannose Membrane Proteins Microsomes, Liver Polyisoprenyl Phosphate Oligosaccharides Polyisoprenyl Phosphate Sugars Polyribosomes Rats Support, U.S. Gov't, P.H.S.
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v26_n2_p123_IdoyagaVargas http://hdl.handle.net/20.500.12110/paper_03008177_v26_n2_p123_IdoyagaVargas
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_03008177_v26_n2_p123_IdoyagaVargas
record_format	dspace
spelling	paper:paper_03008177_v26_n2_p123_IdoyagaVargas2023-06-08T15:27:25Z Oligosaccharide transfer from lipid sugar intermediates to endogenous protein(s) of rat liver microsomal subfractions Burrone, Oscar R. Carminatti, Héctor drug derivative glycoprotein isoprenoid phosphate sugar mannose membrane protein animal article biosynthesis enzymology intracellular membrane liver microsome metabolism polysome rat Animal Glycoproteins Intracellular Membranes Mannose Membrane Proteins Microsomes, Liver Polyisoprenyl Phosphate Oligosaccharides Polyisoprenyl Phosphate Sugars Polyribosomes Rats Support, U.S. Gov't, P.H.S. The subcellular localization and characterization of some of the components involved in the glycosylation of asparagine type glycoproteins was attempted using dolichyl diphosphate [14c]mannose oligosaccharide as precursor of the glycosylation reaction in vitro. Isolated rough and smooth microsomel fractions were able to carry out the transfer of the carbohydrate moiety from lipid oligosaccharide to endogenous protein acceptors. The protein glycosylating activity remained practically the same after stripping the vesicles from their ribosomes or partially releasing their vesicular content. Isolation of polysomes from rough microsomes after glycosylation has taken place, reveals that a large proportion of mannose labeled glycoproteins is in the membranous fraction. The remaining labeled glycoproteins co-sediment with the polysomal fraction. If the isolation is carried out before glycosylation only the membranous fraction shows enzyme activity, whereas the polysomes alone are not able to carry out glycosylation. All these results taken together indicate that the protein glycosylating enzyme is a structural component of the rough and smooth microsomes of rat liver. © 1979 Dr. W. Junk b.v. Publishers. Fil:Burrone, O. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Carminatti, H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1979 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v26_n2_p123_IdoyagaVargas http://hdl.handle.net/20.500.12110/paper_03008177_v26_n2_p123_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	drug derivative glycoprotein isoprenoid phosphate sugar mannose membrane protein animal article biosynthesis enzymology intracellular membrane liver microsome metabolism polysome rat Animal Glycoproteins Intracellular Membranes Mannose Membrane Proteins Microsomes, Liver Polyisoprenyl Phosphate Oligosaccharides Polyisoprenyl Phosphate Sugars Polyribosomes Rats Support, U.S. Gov't, P.H.S.
spellingShingle	drug derivative glycoprotein isoprenoid phosphate sugar mannose membrane protein animal article biosynthesis enzymology intracellular membrane liver microsome metabolism polysome rat Animal Glycoproteins Intracellular Membranes Mannose Membrane Proteins Microsomes, Liver Polyisoprenyl Phosphate Oligosaccharides Polyisoprenyl Phosphate Sugars Polyribosomes Rats Support, U.S. Gov't, P.H.S. Burrone, Oscar R. Carminatti, Héctor Oligosaccharide transfer from lipid sugar intermediates to endogenous protein(s) of rat liver microsomal subfractions
topic_facet	drug derivative glycoprotein isoprenoid phosphate sugar mannose membrane protein animal article biosynthesis enzymology intracellular membrane liver microsome metabolism polysome rat Animal Glycoproteins Intracellular Membranes Mannose Membrane Proteins Microsomes, Liver Polyisoprenyl Phosphate Oligosaccharides Polyisoprenyl Phosphate Sugars Polyribosomes Rats Support, U.S. Gov't, P.H.S.
description	The subcellular localization and characterization of some of the components involved in the glycosylation of asparagine type glycoproteins was attempted using dolichyl diphosphate [14c]mannose oligosaccharide as precursor of the glycosylation reaction in vitro. Isolated rough and smooth microsomel fractions were able to carry out the transfer of the carbohydrate moiety from lipid oligosaccharide to endogenous protein acceptors. The protein glycosylating activity remained practically the same after stripping the vesicles from their ribosomes or partially releasing their vesicular content. Isolation of polysomes from rough microsomes after glycosylation has taken place, reveals that a large proportion of mannose labeled glycoproteins is in the membranous fraction. The remaining labeled glycoproteins co-sediment with the polysomal fraction. If the isolation is carried out before glycosylation only the membranous fraction shows enzyme activity, whereas the polysomes alone are not able to carry out glycosylation. All these results taken together indicate that the protein glycosylating enzyme is a structural component of the rough and smooth microsomes of rat liver. © 1979 Dr. W. Junk b.v. Publishers.
author	Burrone, Oscar R. Carminatti, Héctor
author_facet	Burrone, Oscar R. Carminatti, Héctor
author_sort	Burrone, Oscar R.
title	Oligosaccharide transfer from lipid sugar intermediates to endogenous protein(s) of rat liver microsomal subfractions
title_short	Oligosaccharide transfer from lipid sugar intermediates to endogenous protein(s) of rat liver microsomal subfractions
title_full	Oligosaccharide transfer from lipid sugar intermediates to endogenous protein(s) of rat liver microsomal subfractions
title_fullStr	Oligosaccharide transfer from lipid sugar intermediates to endogenous protein(s) of rat liver microsomal subfractions
title_full_unstemmed	Oligosaccharide transfer from lipid sugar intermediates to endogenous protein(s) of rat liver microsomal subfractions
title_sort	oligosaccharide transfer from lipid sugar intermediates to endogenous protein(s) of rat liver microsomal subfractions
publishDate	1979
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v26_n2_p123_IdoyagaVargas http://hdl.handle.net/20.500.12110/paper_03008177_v26_n2_p123_IdoyagaVargas
work_keys_str_mv	AT burroneoscarr oligosaccharidetransferfromlipidsugarintermediatestoendogenousproteinsofratlivermicrosomalsubfractions AT carminattihector oligosaccharidetransferfromlipidsugarintermediatestoendogenousproteinsofratlivermicrosomalsubfractions
_version_	1768543420808167424

Oligosaccharide transfer from lipid sugar intermediates to endogenous protein(s) of rat liver microsomal subfractions

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