Subcellular localization, of glucosyl transferases involved in lectin glucosylation in pisum sativum seedlings

Cellular membranes from 4 to 5-days old etiolated pea seedlings were isolated by isopyenic centrifugation. Marker enzymes were used to measure the purity of the subcellular fractions. The formation of dolichy!-P-glucose and of glucosylated lectin was tested in all the fractions. Both activities were...

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Autores principales: Hopp, E.H., Romero, P., Lezica, R.P.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00320781_v20_n6_p1063_Hopp
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spelling todo:paper_00320781_v20_n6_p1063_Hopp2023-10-03T14:44:46Z Subcellular localization, of glucosyl transferases involved in lectin glucosylation in pisum sativum seedlings Hopp, E.H. Romero, P. Lezica, R.P. Glucosyl transferases Glycosylation Lectin biosynthesis Pisum sativum Protein Cellular membranes from 4 to 5-days old etiolated pea seedlings were isolated by isopyenic centrifugation. Marker enzymes were used to measure the purity of the subcellular fractions. The formation of dolichy!-P-glucose and of glucosylated lectin was tested in all the fractions. Both activities were associated with the endoplasmic reticulum fractions. When the membranes were prepared in the presence of EDTA, a shift in both activities to a lower density in the gradient was observed.These results are in agreement with the current assumption that glycosylation of proteins via lipid-linked sugars is a cotranslational process. © 1979 Oxford University Press. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00320781_v20_n6_p1063_Hopp
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Glucosyl transferases
Glycosylation
Lectin biosynthesis
Pisum sativum
Protein
spellingShingle Glucosyl transferases
Glycosylation
Lectin biosynthesis
Pisum sativum
Protein
Hopp, E.H.
Romero, P.
Lezica, R.P.
Subcellular localization, of glucosyl transferases involved in lectin glucosylation in pisum sativum seedlings
topic_facet Glucosyl transferases
Glycosylation
Lectin biosynthesis
Pisum sativum
Protein
description Cellular membranes from 4 to 5-days old etiolated pea seedlings were isolated by isopyenic centrifugation. Marker enzymes were used to measure the purity of the subcellular fractions. The formation of dolichy!-P-glucose and of glucosylated lectin was tested in all the fractions. Both activities were associated with the endoplasmic reticulum fractions. When the membranes were prepared in the presence of EDTA, a shift in both activities to a lower density in the gradient was observed.These results are in agreement with the current assumption that glycosylation of proteins via lipid-linked sugars is a cotranslational process. © 1979 Oxford University Press.
format JOUR
author Hopp, E.H.
Romero, P.
Lezica, R.P.
author_facet Hopp, E.H.
Romero, P.
Lezica, R.P.
author_sort Hopp, E.H.
title Subcellular localization, of glucosyl transferases involved in lectin glucosylation in pisum sativum seedlings
title_short Subcellular localization, of glucosyl transferases involved in lectin glucosylation in pisum sativum seedlings
title_full Subcellular localization, of glucosyl transferases involved in lectin glucosylation in pisum sativum seedlings
title_fullStr Subcellular localization, of glucosyl transferases involved in lectin glucosylation in pisum sativum seedlings
title_full_unstemmed Subcellular localization, of glucosyl transferases involved in lectin glucosylation in pisum sativum seedlings
title_sort subcellular localization, of glucosyl transferases involved in lectin glucosylation in pisum sativum seedlings
url http://hdl.handle.net/20.500.12110/paper_00320781_v20_n6_p1063_Hopp
work_keys_str_mv AT hoppeh subcellularlocalizationofglucosyltransferasesinvolvedinlectinglucosylationinpisumsativumseedlings
AT romerop subcellularlocalizationofglucosyltransferasesinvolvedinlectinglucosylationinpisumsativumseedlings
AT lezicarp subcellularlocalizationofglucosyltransferasesinvolvedinlectinglucosylationinpisumsativumseedlings
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