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Abstract:

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

Registro:

Documento: Artículo
Título:Rate of Protein Glycosylation in Rat Cerebral Cortex
Autor:Aplerin, D.M.; Idoyaga-Vargas, V.P.; Carminatti, H.
Filiación:Instituto de Investigaciones Bioquímicas "Fundación Campomar" and Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina
Palabras clave: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
Año:1986
Volumen:47
Número:2
Página de inicio:355
Página de fin:362
DOI: http://dx.doi.org/10.1111/j.1471-4159.1986.tb04509.x
Título revista:Journal of Neurochemistry
Título revista abreviado:J. Neurochem.
ISSN:00223042
CAS:Glucose, 50-99-7; Glycoproteins; Leucine, 61-90-5; Mannose, 31103-86-3; Nerve Tissue Proteins; Tritium, 10028-17-8
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00223042_v47_n2_p355_Aplerin

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Citas:

---------- APA ----------
Aplerin, D.M., Idoyaga-Vargas, V.P. & Carminatti, H. (1986) . Rate of Protein Glycosylation in Rat Cerebral Cortex. Journal of Neurochemistry, 47(2), 355-362.
http://dx.doi.org/10.1111/j.1471-4159.1986.tb04509.x
---------- CHICAGO ----------
Aplerin, D.M., Idoyaga-Vargas, V.P., Carminatti, H. "Rate of Protein Glycosylation in Rat Cerebral Cortex" . Journal of Neurochemistry 47, no. 2 (1986) : 355-362.
http://dx.doi.org/10.1111/j.1471-4159.1986.tb04509.x
---------- MLA ----------
Aplerin, D.M., Idoyaga-Vargas, V.P., Carminatti, H. "Rate of Protein Glycosylation in Rat Cerebral Cortex" . Journal of Neurochemistry, vol. 47, no. 2, 1986, pp. 355-362.
http://dx.doi.org/10.1111/j.1471-4159.1986.tb04509.x
---------- VANCOUVER ----------
Aplerin, D.M., Idoyaga-Vargas, V.P., Carminatti, H. Rate of Protein Glycosylation in Rat Cerebral Cortex. J. Neurochem. 1986;47(2):355-362.
http://dx.doi.org/10.1111/j.1471-4159.1986.tb04509.x