Microsomal Glucosidases of Rat Liver. Partial Purification and Inhibition by Disaccharides

Further work on microsomal glucosidases of rat liver has confirmed that at least two enzymes are involved in the removal of glucose from the glucose‐containing oligosaccharide. One acts on the oligosaccharide containing three glucose residues and another on the oligosaccharide which has one or two g...

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Autores principales: UGALDE, R.A., STANELONI, R.J., LELOIR, L.F.
Formato: JOUR
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rat
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00142956_v113_n1_p97_UGALDE
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spelling todo:paper_00142956_v113_n1_p97_UGALDE2023-10-03T14:11:46Z Microsomal Glucosidases of Rat Liver. Partial Purification and Inhibition by Disaccharides UGALDE, R.A. STANELONI, R.J. LELOIR, L.F. disaccharide glucosidase glycoprotein isoprenoid phosphate sugar kojibiose animal article enzymology isolation and purification liver microsome metabolism rat Animal Disaccharides Glucosidases Glycoproteins Microsomes, Liver Polyisoprenyl Phosphate Oligosaccharides Rats Further work on microsomal glucosidases of rat liver has confirmed that at least two enzymes are involved in the removal of glucose from the glucose‐containing oligosaccharide. One acts on the oligosaccharide containing three glucose residues and another on the oligosaccharide which has one or two glucoses. The glucosidase which acts on (Glc)2(Man)9(GlcNAc)2 could be purified with a ConcanavalinA—Sepharose column followed by electrofocusing. This purified preparation was active on the oligosaccharide containing one or two glucoses. Heat inactivation and inhibition by disaccharides was parallel for both activities. Inhibition of the glucosidase active on (Glc)3(Man)9(GlcNAc)2 was obtained with kojibiose which has an α 1–2 linkage, while the glucosidase acting on (Glc)1–2(Man)9‐(GlcNAc)2 was inhibited by nigerose (α 1–3 linkage), maltose (α 1–4 linkage) and glucose at a higher concentration. None of the β anomers inhibited. These results are consistent with an α configuration of the three glucoses of the dolichyl‐dinhosphate‐linked oligosaccharide. Kojibiose was found to inhibit glucosidase action not only on the free oligosaccharide but also on protein‐bound one. Copyright © 1980, Wiley Blackwell. All rights reserved JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00142956_v113_n1_p97_UGALDE
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic disaccharide
glucosidase
glycoprotein
isoprenoid phosphate sugar
kojibiose
animal
article
enzymology
isolation and purification
liver microsome
metabolism
rat
Animal
Disaccharides
Glucosidases
Glycoproteins
Microsomes, Liver
Polyisoprenyl Phosphate Oligosaccharides
Rats
spellingShingle disaccharide
glucosidase
glycoprotein
isoprenoid phosphate sugar
kojibiose
animal
article
enzymology
isolation and purification
liver microsome
metabolism
rat
Animal
Disaccharides
Glucosidases
Glycoproteins
Microsomes, Liver
Polyisoprenyl Phosphate Oligosaccharides
Rats
UGALDE, R.A.
STANELONI, R.J.
LELOIR, L.F.
Microsomal Glucosidases of Rat Liver. Partial Purification and Inhibition by Disaccharides
topic_facet disaccharide
glucosidase
glycoprotein
isoprenoid phosphate sugar
kojibiose
animal
article
enzymology
isolation and purification
liver microsome
metabolism
rat
Animal
Disaccharides
Glucosidases
Glycoproteins
Microsomes, Liver
Polyisoprenyl Phosphate Oligosaccharides
Rats
description Further work on microsomal glucosidases of rat liver has confirmed that at least two enzymes are involved in the removal of glucose from the glucose‐containing oligosaccharide. One acts on the oligosaccharide containing three glucose residues and another on the oligosaccharide which has one or two glucoses. The glucosidase which acts on (Glc)2(Man)9(GlcNAc)2 could be purified with a ConcanavalinA—Sepharose column followed by electrofocusing. This purified preparation was active on the oligosaccharide containing one or two glucoses. Heat inactivation and inhibition by disaccharides was parallel for both activities. Inhibition of the glucosidase active on (Glc)3(Man)9(GlcNAc)2 was obtained with kojibiose which has an α 1–2 linkage, while the glucosidase acting on (Glc)1–2(Man)9‐(GlcNAc)2 was inhibited by nigerose (α 1–3 linkage), maltose (α 1–4 linkage) and glucose at a higher concentration. None of the β anomers inhibited. These results are consistent with an α configuration of the three glucoses of the dolichyl‐dinhosphate‐linked oligosaccharide. Kojibiose was found to inhibit glucosidase action not only on the free oligosaccharide but also on protein‐bound one. Copyright © 1980, Wiley Blackwell. All rights reserved
format JOUR
author UGALDE, R.A.
STANELONI, R.J.
LELOIR, L.F.
author_facet UGALDE, R.A.
STANELONI, R.J.
LELOIR, L.F.
author_sort UGALDE, R.A.
title Microsomal Glucosidases of Rat Liver. Partial Purification and Inhibition by Disaccharides
title_short Microsomal Glucosidases of Rat Liver. Partial Purification and Inhibition by Disaccharides
title_full Microsomal Glucosidases of Rat Liver. Partial Purification and Inhibition by Disaccharides
title_fullStr Microsomal Glucosidases of Rat Liver. Partial Purification and Inhibition by Disaccharides
title_full_unstemmed Microsomal Glucosidases of Rat Liver. Partial Purification and Inhibition by Disaccharides
title_sort microsomal glucosidases of rat liver. partial purification and inhibition by disaccharides
url http://hdl.handle.net/20.500.12110/paper_00142956_v113_n1_p97_UGALDE
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AT stanelonirj microsomalglucosidasesofratliverpartialpurificationandinhibitionbydisaccharides
AT leloirlf microsomalglucosidasesofratliverpartialpurificationandinhibitionbydisaccharides
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