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spelling paper:paper_00142956_v75_n1_p171_PARODI2023-06-08T14:36:45Z Synthesis of Glucosyl‐Dolichol Derivatives in Bakers' Yeast and Their Role in Protein Glycosylation n acetylglucosamine radioisotope chymotrypsin diterpene dolichol glucoside glycoside mannosidase oligosaccharide papain phospholipid pronase uridine diphosphate glucose dolichol phosphate glucose in vitro study microorganism saccharomyces cerevisiae theoretical study uridine diphosphate glucose c 14 animal article biosynthesis liver metabolism Saccharomyces cerevisiae species difference Animal Chymotrypsin Diterpenes Dolichol Glucosides Glycosides Liver Mannosidases Oligosaccharides Papain Phospholipids Pronase Saccharomyces cerevisiae Species Specificity Support, U.S. Gov't, P.H.S. Uridine Diphosphate Glucose Two substances soluble in organic solvents were synthesized when UDP‐[14C]glucose was incubated with a bakers' yeast particulate fraction. One of them was identified as dolichol‐P‐glucose by several analytical criteria. The only difference that could be found between the yeast and liver dolichol‐P‐glucose was the molecular size of their dolichol moieties. According to the molecular weight of the sodium deoxycholate inclusion compounds measured by gel filtration, yeast dolichol‐P‐glucose contained 15–16 isoprene units. This is in accordance with the known structure of yeast dolichol. The other product soluble in organic solvents was identified as steryl glucoside. Incubation of dolichol‐P‐[14C]glucose with the yeast particulate fraction led to the transfer of glucose residues to an endogenous acceptor. From evidence gathered in experiments performed with the labelled compound it is suggested that as in animal tissues the glucosylated endogenous acceptor contains two N‐acetylhexosamine (possibly N‐acetylglucosamine) and several mannose and glucose residues joined to yeast dolichol through a pyrophosphate bridge. Glycosylation of endogenous proteins was detected when a similar glucosylated endogenous acceptor from rat liver was incubated with the yeast particulate fraction. It is suggested that the following reactions of glucose transfer take place in a yeast particulate fraction: Dolichol‐P+UDP‐glucose → Dolichol‐P‐glucose + UDP Dolichol‐P‐glucose + Dolichol‐P‐P‐(N‐acetylglucosamine)2 (mannose)x→ Dolichol‐P‐P‐(N‐acetylglucosamine)2 (mannose)x (glucose)y+ Dolichol‐P Dolichol‐P‐P‐(N‐acetylglucosamine)2 (mannose)x (glucose)y+ protein → Protein‐(N‐acetylglucosamine)2 (mannose)x (glucose)y+ Dolichol‐P‐P. Copyright © 1977, Wiley Blackwell. All rights reserved 1977 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v75_n1_p171_PARODI http://hdl.handle.net/20.500.12110/paper_00142956_v75_n1_p171_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 n acetylglucosamine
radioisotope
chymotrypsin
diterpene
dolichol
glucoside
glycoside
mannosidase
oligosaccharide
papain
phospholipid
pronase
uridine diphosphate glucose
dolichol phosphate glucose
in vitro study
microorganism
saccharomyces cerevisiae
theoretical study
uridine diphosphate glucose c 14
animal
article
biosynthesis
liver
metabolism
Saccharomyces cerevisiae
species difference
Animal
Chymotrypsin
Diterpenes
Dolichol
Glucosides
Glycosides
Liver
Mannosidases
Oligosaccharides
Papain
Phospholipids
Pronase
Saccharomyces cerevisiae
Species Specificity
Support, U.S. Gov't, P.H.S.
Uridine Diphosphate Glucose
spellingShingle n acetylglucosamine
radioisotope
chymotrypsin
diterpene
dolichol
glucoside
glycoside
mannosidase
oligosaccharide
papain
phospholipid
pronase
uridine diphosphate glucose
dolichol phosphate glucose
in vitro study
microorganism
saccharomyces cerevisiae
theoretical study
uridine diphosphate glucose c 14
animal
article
biosynthesis
liver
metabolism
Saccharomyces cerevisiae
species difference
Animal
Chymotrypsin
Diterpenes
Dolichol
Glucosides
Glycosides
Liver
Mannosidases
Oligosaccharides
Papain
Phospholipids
Pronase
Saccharomyces cerevisiae
Species Specificity
Support, U.S. Gov't, P.H.S.
Uridine Diphosphate Glucose
Synthesis of Glucosyl‐Dolichol Derivatives in Bakers' Yeast and Their Role in Protein Glycosylation
topic_facet n acetylglucosamine
radioisotope
chymotrypsin
diterpene
dolichol
glucoside
glycoside
mannosidase
oligosaccharide
papain
phospholipid
pronase
uridine diphosphate glucose
dolichol phosphate glucose
in vitro study
microorganism
saccharomyces cerevisiae
theoretical study
uridine diphosphate glucose c 14
animal
article
biosynthesis
liver
metabolism
Saccharomyces cerevisiae
species difference
Animal
Chymotrypsin
Diterpenes
Dolichol
Glucosides
Glycosides
Liver
Mannosidases
Oligosaccharides
Papain
Phospholipids
Pronase
Saccharomyces cerevisiae
Species Specificity
Support, U.S. Gov't, P.H.S.
Uridine Diphosphate Glucose
description Two substances soluble in organic solvents were synthesized when UDP‐[14C]glucose was incubated with a bakers' yeast particulate fraction. One of them was identified as dolichol‐P‐glucose by several analytical criteria. The only difference that could be found between the yeast and liver dolichol‐P‐glucose was the molecular size of their dolichol moieties. According to the molecular weight of the sodium deoxycholate inclusion compounds measured by gel filtration, yeast dolichol‐P‐glucose contained 15–16 isoprene units. This is in accordance with the known structure of yeast dolichol. The other product soluble in organic solvents was identified as steryl glucoside. Incubation of dolichol‐P‐[14C]glucose with the yeast particulate fraction led to the transfer of glucose residues to an endogenous acceptor. From evidence gathered in experiments performed with the labelled compound it is suggested that as in animal tissues the glucosylated endogenous acceptor contains two N‐acetylhexosamine (possibly N‐acetylglucosamine) and several mannose and glucose residues joined to yeast dolichol through a pyrophosphate bridge. Glycosylation of endogenous proteins was detected when a similar glucosylated endogenous acceptor from rat liver was incubated with the yeast particulate fraction. It is suggested that the following reactions of glucose transfer take place in a yeast particulate fraction: Dolichol‐P+UDP‐glucose → Dolichol‐P‐glucose + UDP Dolichol‐P‐glucose + Dolichol‐P‐P‐(N‐acetylglucosamine)2 (mannose)x→ Dolichol‐P‐P‐(N‐acetylglucosamine)2 (mannose)x (glucose)y+ Dolichol‐P Dolichol‐P‐P‐(N‐acetylglucosamine)2 (mannose)x (glucose)y+ protein → Protein‐(N‐acetylglucosamine)2 (mannose)x (glucose)y+ Dolichol‐P‐P. Copyright © 1977, Wiley Blackwell. All rights reserved
title Synthesis of Glucosyl‐Dolichol Derivatives in Bakers' Yeast and Their Role in Protein Glycosylation
title_short Synthesis of Glucosyl‐Dolichol Derivatives in Bakers' Yeast and Their Role in Protein Glycosylation
title_full Synthesis of Glucosyl‐Dolichol Derivatives in Bakers' Yeast and Their Role in Protein Glycosylation
title_fullStr Synthesis of Glucosyl‐Dolichol Derivatives in Bakers' Yeast and Their Role in Protein Glycosylation
title_full_unstemmed Synthesis of Glucosyl‐Dolichol Derivatives in Bakers' Yeast and Their Role in Protein Glycosylation
title_sort synthesis of glucosyl‐dolichol derivatives in bakers' yeast and their role in protein glycosylation
publishDate 1977
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v75_n1_p171_PARODI
http://hdl.handle.net/20.500.12110/paper_00142956_v75_n1_p171_PARODI
_version_ 1768544485367611392