Glycosylation of endogenous proteins through dolichol derivatives in reticulocyte plasma membranes

It has been found that rabbit reticulocyte plasma membranes contain the enzymatic activities responsible for the synthesis of all the polyprenol-bound sugars that are intermediates in the glycosylation of proteins. The final reaction in which an oligosaccharide is transferred from a dolichol pyropho...

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Detalles Bibliográficos
Autores principales:	Parodi, A.J., Martin-Barrientos, J.
Formato:	JOUR
Materias:	protein cell membrane dolichol derivative glycosylation in vitro study reticulocyte theoretical study Animal Cell Membrane Diterpenes Dolichol Dolichol Phosphates Erythrocyte Membrane Glycoproteins Molecular Weight Reticulocytes Support, U.S. Gov't, P.H.S. Uridine Diphosphate Glucose Uridine Diphosphate N-Acetylglucosamine
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_03044165_v500_n1_p80_Parodi
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_03044165_v500_n1_p80_Parodi
record_format	dspace
spelling	todo:paper_03044165_v500_n1_p80_Parodi2023-10-03T15:20:48Z Glycosylation of endogenous proteins through dolichol derivatives in reticulocyte plasma membranes Parodi, A.J. Martin-Barrientos, J. protein cell membrane dolichol derivative glycosylation in vitro study reticulocyte theoretical study Animal Cell Membrane Diterpenes Dolichol Dolichol Phosphates Erythrocyte Membrane Glycoproteins Molecular Weight Reticulocytes Support, U.S. Gov't, P.H.S. Uridine Diphosphate Glucose Uridine Diphosphate N-Acetylglucosamine It has been found that rabbit reticulocyte plasma membranes contain the enzymatic activities responsible for the synthesis of all the polyprenol-bound sugars that are intermediates in the glycosylation of proteins. The final reaction in which an oligosaccharide is transferred from a dolichol pyrophosphate derivative to an endogenous protein was detected in reticulocyte but not in erythrocyte plasma membranes. © 1977. Fil:Parodi, A.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03044165_v500_n1_p80_Parodi
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	protein cell membrane dolichol derivative glycosylation in vitro study reticulocyte theoretical study Animal Cell Membrane Diterpenes Dolichol Dolichol Phosphates Erythrocyte Membrane Glycoproteins Molecular Weight Reticulocytes Support, U.S. Gov't, P.H.S. Uridine Diphosphate Glucose Uridine Diphosphate N-Acetylglucosamine
spellingShingle	protein cell membrane dolichol derivative glycosylation in vitro study reticulocyte theoretical study Animal Cell Membrane Diterpenes Dolichol Dolichol Phosphates Erythrocyte Membrane Glycoproteins Molecular Weight Reticulocytes Support, U.S. Gov't, P.H.S. Uridine Diphosphate Glucose Uridine Diphosphate N-Acetylglucosamine Parodi, A.J. Martin-Barrientos, J. Glycosylation of endogenous proteins through dolichol derivatives in reticulocyte plasma membranes
topic_facet	protein cell membrane dolichol derivative glycosylation in vitro study reticulocyte theoretical study Animal Cell Membrane Diterpenes Dolichol Dolichol Phosphates Erythrocyte Membrane Glycoproteins Molecular Weight Reticulocytes Support, U.S. Gov't, P.H.S. Uridine Diphosphate Glucose Uridine Diphosphate N-Acetylglucosamine
description	It has been found that rabbit reticulocyte plasma membranes contain the enzymatic activities responsible for the synthesis of all the polyprenol-bound sugars that are intermediates in the glycosylation of proteins. The final reaction in which an oligosaccharide is transferred from a dolichol pyrophosphate derivative to an endogenous protein was detected in reticulocyte but not in erythrocyte plasma membranes. © 1977.
format	JOUR
author	Parodi, A.J. Martin-Barrientos, J.
author_facet	Parodi, A.J. Martin-Barrientos, J.
author_sort	Parodi, A.J.
title	Glycosylation of endogenous proteins through dolichol derivatives in reticulocyte plasma membranes
title_short	Glycosylation of endogenous proteins through dolichol derivatives in reticulocyte plasma membranes
title_full	Glycosylation of endogenous proteins through dolichol derivatives in reticulocyte plasma membranes
title_fullStr	Glycosylation of endogenous proteins through dolichol derivatives in reticulocyte plasma membranes
title_full_unstemmed	Glycosylation of endogenous proteins through dolichol derivatives in reticulocyte plasma membranes
title_sort	glycosylation of endogenous proteins through dolichol derivatives in reticulocyte plasma membranes
url	http://hdl.handle.net/20.500.12110/paper_03044165_v500_n1_p80_Parodi
work_keys_str_mv	AT parodiaj glycosylationofendogenousproteinsthroughdolicholderivativesinreticulocyteplasmamembranes AT martinbarrientosj glycosylationofendogenousproteinsthroughdolicholderivativesinreticulocyteplasmamembranes
_version_	1807321668122574848

Glycosylation of endogenous proteins through dolichol derivatives in reticulocyte plasma membranes

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