Rate of Protein Glycosylation in Rat Cerebral Cortex

Abstract: Quantitative aspects of the pathway leading to the formation of asparagine‐linked oligosaccharides were investigated in rat cerebral cortex. Steady‐state labeling conditions were achieved with [2‐3H]mannose by developing a micromethod of incubation of cerebral cortex particles in the prese...

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Autor principal: Carminatti, Héctor
Publicado: 1986
Materias:
rat
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00223042_v47_n2_p355_Aplerin
http://hdl.handle.net/20.500.12110/paper_00223042_v47_n2_p355_Aplerin
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spelling paper:paper_00223042_v47_n2_p355_Aplerin2023-06-08T14:49:07Z Rate of Protein Glycosylation in Rat Cerebral Cortex Carminatti, Héctor Cerebral cortex Development Glycosylation rate animal cell brain cortex central nervous system mannose h 3 nonhuman priority journal protein glycosylation rat Aging Animal Cerebral Cortex Comparative Study Diffusion Glucose Glycoproteins Kinetics Leucine Mannose Nerve Tissue Proteins Rats Rats, Inbred Strains Support, Non-U.S. Gov't Tritium Abstract: Quantitative aspects of the pathway leading to the formation of asparagine‐linked oligosaccharides were investigated in rat cerebral cortex. Steady‐state labeling conditions were achieved with [2‐3H]mannose by developing a micromethod of incubation of cerebral cortex particles in the presence of physiological concentrations of glucose (1 g/L). The rate of [2‐3H]mannose uptake and incorporation into protein was markedly affected when the concentration of glucose was lowered to 0.05 g/L. It was found that in the presence of glucose (1 g/L), a minor fraction of the utilized [2‐3H]mannose is used in glyco‐protein formation and the remaining labeled sugar enters the other major metabolic pathways, generating tritiated water which is rapidly exchanged with that of the medium. Under these conditions, the intracellular isotopic dilution of [2‐3H]mannose‐labeled precursors was calculated to be about 11.5‐fold. These data allow determination of the rate of the net transfer of mannose into proteins. Comparison of the rate of glycosylation between 5‐ and 30‐day‐old cerebral cortex revealed a striking difference: 2.1 and 0.3 ng of mannose/mg protein/h, respectively. Copyright © 1986, Wiley Blackwell. All rights reserved Fil:Carminatti, H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1986 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00223042_v47_n2_p355_Aplerin http://hdl.handle.net/20.500.12110/paper_00223042_v47_n2_p355_Aplerin
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Cerebral cortex
Development
Glycosylation rate
animal cell
brain cortex
central nervous system
mannose h 3
nonhuman
priority journal
protein glycosylation
rat
Aging
Animal
Cerebral Cortex
Comparative Study
Diffusion
Glucose
Glycoproteins
Kinetics
Leucine
Mannose
Nerve Tissue Proteins
Rats
Rats, Inbred Strains
Support, Non-U.S. Gov't
Tritium
spellingShingle Cerebral cortex
Development
Glycosylation rate
animal cell
brain cortex
central nervous system
mannose h 3
nonhuman
priority journal
protein glycosylation
rat
Aging
Animal
Cerebral Cortex
Comparative Study
Diffusion
Glucose
Glycoproteins
Kinetics
Leucine
Mannose
Nerve Tissue Proteins
Rats
Rats, Inbred Strains
Support, Non-U.S. Gov't
Tritium
Carminatti, Héctor
Rate of Protein Glycosylation in Rat Cerebral Cortex
topic_facet Cerebral cortex
Development
Glycosylation rate
animal cell
brain cortex
central nervous system
mannose h 3
nonhuman
priority journal
protein glycosylation
rat
Aging
Animal
Cerebral Cortex
Comparative Study
Diffusion
Glucose
Glycoproteins
Kinetics
Leucine
Mannose
Nerve Tissue Proteins
Rats
Rats, Inbred Strains
Support, Non-U.S. Gov't
Tritium
description Abstract: Quantitative aspects of the pathway leading to the formation of asparagine‐linked oligosaccharides were investigated in rat cerebral cortex. Steady‐state labeling conditions were achieved with [2‐3H]mannose by developing a micromethod of incubation of cerebral cortex particles in the presence of physiological concentrations of glucose (1 g/L). The rate of [2‐3H]mannose uptake and incorporation into protein was markedly affected when the concentration of glucose was lowered to 0.05 g/L. It was found that in the presence of glucose (1 g/L), a minor fraction of the utilized [2‐3H]mannose is used in glyco‐protein formation and the remaining labeled sugar enters the other major metabolic pathways, generating tritiated water which is rapidly exchanged with that of the medium. Under these conditions, the intracellular isotopic dilution of [2‐3H]mannose‐labeled precursors was calculated to be about 11.5‐fold. These data allow determination of the rate of the net transfer of mannose into proteins. Comparison of the rate of glycosylation between 5‐ and 30‐day‐old cerebral cortex revealed a striking difference: 2.1 and 0.3 ng of mannose/mg protein/h, respectively. Copyright © 1986, Wiley Blackwell. All rights reserved
author Carminatti, Héctor
author_facet Carminatti, Héctor
author_sort Carminatti, Héctor
title Rate of Protein Glycosylation in Rat Cerebral Cortex
title_short Rate of Protein Glycosylation in Rat Cerebral Cortex
title_full Rate of Protein Glycosylation in Rat Cerebral Cortex
title_fullStr Rate of Protein Glycosylation in Rat Cerebral Cortex
title_full_unstemmed Rate of Protein Glycosylation in Rat Cerebral Cortex
title_sort rate of protein glycosylation in rat cerebral cortex
publishDate 1986
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00223042_v47_n2_p355_Aplerin
http://hdl.handle.net/20.500.12110/paper_00223042_v47_n2_p355_Aplerin
work_keys_str_mv AT carminattihector rateofproteinglycosylationinratcerebralcortex
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