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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1980
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v113_n1_p97_UGALDE http://hdl.handle.net/20.500.12110/paper_00142956_v113_n1_p97_UGALDE |
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paper:paper_00142956_v113_n1_p97_UGALDE2023-06-08T14:36:36Z Microsomal Glucosidases of Rat Liver. Partial Purification and Inhibition by Disaccharides 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 1980 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v113_n1_p97_UGALDE 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 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 |
| 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 |
| publishDate |
1980 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v113_n1_p97_UGALDE http://hdl.handle.net/20.500.12110/paper_00142956_v113_n1_p97_UGALDE |
| _version_ |
1768546285112000512 |