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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1979
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00320781_v20_n6_p1063_Hopp http://hdl.handle.net/20.500.12110/paper_00320781_v20_n6_p1063_Hopp |
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paper:paper_00320781_v20_n6_p1063_Hopp2023-06-08T14:59:53Z Subcellular localization, of glucosyl transferases involved in lectin glucosylation in pisum sativum seedlings 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. 1979 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00320781_v20_n6_p1063_Hopp 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 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. |
| 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 |
| publishDate |
1979 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00320781_v20_n6_p1063_Hopp http://hdl.handle.net/20.500.12110/paper_00320781_v20_n6_p1063_Hopp |
| _version_ |
1768542257146757120 |