Enzymatic synthesis of polyprenol monophosphate mannose in insects
The microsomal fraction of insects was found to contain an enzyme which transfers mannose from guanosine diphosphate mannose to an endogenous or exogenous insect lipid and to other acceptors such as dolichol monophosphate or ficaprenol monophosphate. This activity depended on the presence of Triton...
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todo:paper_03008177_v16_n2-3_p127_Belocopitow2023-10-03T15:17:42Z Enzymatic synthesis of polyprenol monophosphate mannose in insects Belocopitow, E. Marechal, L.R. Quesada Allue, L.A. dolichol phosphate mannose arthropod in vitro study microsome polyprenyl phosphate theoretical study Animal Cobalt Diptera Enzyme Activation Hexosephosphates Hexosyltransferases Hydrogen-Ion Concentration Kinetics Larva Magnesium Manganese Mannosyltransferases Microsomes Phospholipids Polyethylene Glycols Pupa Temperature Terpenes Triatoma Triatominae The microsomal fraction of insects was found to contain an enzyme which transfers mannose from guanosine diphosphate mannose to an endogenous or exogenous insect lipid and to other acceptors such as dolichol monophosphate or ficaprenol monophosphate. This activity depended on the presence of Triton X-100 and magnesium ions, the optimal concentration of the latter being 10mM. The optimal temperature of the reaction was 25 °C and the maximal activity was obtained at pH 7.9. The mannolipid formed behaved as a monophosphodiester when chromatographed on DEAE-cellulose. Weak acid treatment of the product liberated mannose. Its behaviour both on thin layer and Sephadex G-150 chromatography would indicate the presence of a number of isoprenyl units similar to the dolichol and different from the ficaprenol derivative. Stability to phenol treatment indicated that the lipid fraction of the mannolipid is an ±-saturated polyprenol phosphate similar to dolichol monophosphate. © 1977 Dr. W. Junk b.v. Publishers. Fil:Belocopitow, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Quesada Allue, L.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p127_Belocopitow |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
dolichol phosphate mannose arthropod in vitro study microsome polyprenyl phosphate theoretical study Animal Cobalt Diptera Enzyme Activation Hexosephosphates Hexosyltransferases Hydrogen-Ion Concentration Kinetics Larva Magnesium Manganese Mannosyltransferases Microsomes Phospholipids Polyethylene Glycols Pupa Temperature Terpenes Triatoma Triatominae |
spellingShingle |
dolichol phosphate mannose arthropod in vitro study microsome polyprenyl phosphate theoretical study Animal Cobalt Diptera Enzyme Activation Hexosephosphates Hexosyltransferases Hydrogen-Ion Concentration Kinetics Larva Magnesium Manganese Mannosyltransferases Microsomes Phospholipids Polyethylene Glycols Pupa Temperature Terpenes Triatoma Triatominae Belocopitow, E. Marechal, L.R. Quesada Allue, L.A. Enzymatic synthesis of polyprenol monophosphate mannose in insects |
topic_facet |
dolichol phosphate mannose arthropod in vitro study microsome polyprenyl phosphate theoretical study Animal Cobalt Diptera Enzyme Activation Hexosephosphates Hexosyltransferases Hydrogen-Ion Concentration Kinetics Larva Magnesium Manganese Mannosyltransferases Microsomes Phospholipids Polyethylene Glycols Pupa Temperature Terpenes Triatoma Triatominae |
description |
The microsomal fraction of insects was found to contain an enzyme which transfers mannose from guanosine diphosphate mannose to an endogenous or exogenous insect lipid and to other acceptors such as dolichol monophosphate or ficaprenol monophosphate. This activity depended on the presence of Triton X-100 and magnesium ions, the optimal concentration of the latter being 10mM. The optimal temperature of the reaction was 25 °C and the maximal activity was obtained at pH 7.9. The mannolipid formed behaved as a monophosphodiester when chromatographed on DEAE-cellulose. Weak acid treatment of the product liberated mannose. Its behaviour both on thin layer and Sephadex G-150 chromatography would indicate the presence of a number of isoprenyl units similar to the dolichol and different from the ficaprenol derivative. Stability to phenol treatment indicated that the lipid fraction of the mannolipid is an ±-saturated polyprenol phosphate similar to dolichol monophosphate. © 1977 Dr. W. Junk b.v. Publishers. |
format |
JOUR |
author |
Belocopitow, E. Marechal, L.R. Quesada Allue, L.A. |
author_facet |
Belocopitow, E. Marechal, L.R. Quesada Allue, L.A. |
author_sort |
Belocopitow, E. |
title |
Enzymatic synthesis of polyprenol monophosphate mannose in insects |
title_short |
Enzymatic synthesis of polyprenol monophosphate mannose in insects |
title_full |
Enzymatic synthesis of polyprenol monophosphate mannose in insects |
title_fullStr |
Enzymatic synthesis of polyprenol monophosphate mannose in insects |
title_full_unstemmed |
Enzymatic synthesis of polyprenol monophosphate mannose in insects |
title_sort |
enzymatic synthesis of polyprenol monophosphate mannose in insects |
url |
http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p127_Belocopitow |
work_keys_str_mv |
AT belocopitowe enzymaticsynthesisofpolyprenolmonophosphatemannoseininsects AT marechallr enzymaticsynthesisofpolyprenolmonophosphatemannoseininsects AT quesadaalluela enzymaticsynthesisofpolyprenolmonophosphatemannoseininsects |
_version_ |
1807317633839661056 |