Porphyrin biosynthesis in the soybean callus system-XVII. Effect of monovalent and divalent cations on the activity of succinyl CoA synthetase

1. 1. The effect on the activity of soybean callus Succinyl CoA Synthetase of EDTA, 8-OH quinoline, o-phenantroline, α,α $ ́dipyridyl, sodium azide and sodium cyanide was assayed. EDTA completely inhibit the enzyme, cyanide only diminished its activity 30%, and the other compounds significantly enha...

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Autores principales: De Xifra, E.A.W., Del C. Batlle, A.M.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p717_DeXifra
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spelling todo:paper_0020711X_v12_n5-6_p717_DeXifra2023-10-03T14:17:38Z Porphyrin biosynthesis in the soybean callus system-XVII. Effect of monovalent and divalent cations on the activity of succinyl CoA synthetase De Xifra, E.A.W. Del C. Batlle, A.M. magnesium manganese porphyrin succinyl coenzyme a synthetase animal experiment higher plant Cations, Divalent Cations, Monovalent Coenzyme A Ligases Kinetics Plants Porphyrins Soybeans Succinate-CoA Ligases Support, Non-U.S. Gov't 1. 1. The effect on the activity of soybean callus Succinyl CoA Synthetase of EDTA, 8-OH quinoline, o-phenantroline, α,α $ ́dipyridyl, sodium azide and sodium cyanide was assayed. EDTA completely inhibit the enzyme, cyanide only diminished its activity 30%, and the other compounds significantly enhanced Succinyl CoA Synthetase activity. 2. 2. The action of various divalent cation chlorides was studied. The enzyme activation capacities of Mn2+ and Mg2+ were rather similar at all concentrations tested. At 4 and 5 mM Co2+ activates the enzyme more than Mg2+ and Mn2+. Complete inactivation was produced by Pb2+and Hg2+ at concentrations as low as 1 mM. Ca2+, Zn2+, Fe2+ and Cd2+ could not replace Mg2+ either, instead they inhibited Succinyl CoA Synthetase. 3. 3. The assay with the monovalent cations chlorides K +, NH+ 4, Na+ and Li+ showed that maximum activation for the first three was found at 50-60 mM while Li+ had no effect. Increasing concentrations of these cations progressivey progressively inhibited enzyme activity. © 1980. Fil:Del C. Batlle, A.M. 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_0020711X_v12_n5-6_p717_DeXifra
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic magnesium
manganese
porphyrin
succinyl coenzyme a synthetase
animal experiment
higher plant
Cations, Divalent
Cations, Monovalent
Coenzyme A Ligases
Kinetics
Plants
Porphyrins
Soybeans
Succinate-CoA Ligases
Support, Non-U.S. Gov't
spellingShingle magnesium
manganese
porphyrin
succinyl coenzyme a synthetase
animal experiment
higher plant
Cations, Divalent
Cations, Monovalent
Coenzyme A Ligases
Kinetics
Plants
Porphyrins
Soybeans
Succinate-CoA Ligases
Support, Non-U.S. Gov't
De Xifra, E.A.W.
Del C. Batlle, A.M.
Porphyrin biosynthesis in the soybean callus system-XVII. Effect of monovalent and divalent cations on the activity of succinyl CoA synthetase
topic_facet magnesium
manganese
porphyrin
succinyl coenzyme a synthetase
animal experiment
higher plant
Cations, Divalent
Cations, Monovalent
Coenzyme A Ligases
Kinetics
Plants
Porphyrins
Soybeans
Succinate-CoA Ligases
Support, Non-U.S. Gov't
description 1. 1. The effect on the activity of soybean callus Succinyl CoA Synthetase of EDTA, 8-OH quinoline, o-phenantroline, α,α $ ́dipyridyl, sodium azide and sodium cyanide was assayed. EDTA completely inhibit the enzyme, cyanide only diminished its activity 30%, and the other compounds significantly enhanced Succinyl CoA Synthetase activity. 2. 2. The action of various divalent cation chlorides was studied. The enzyme activation capacities of Mn2+ and Mg2+ were rather similar at all concentrations tested. At 4 and 5 mM Co2+ activates the enzyme more than Mg2+ and Mn2+. Complete inactivation was produced by Pb2+and Hg2+ at concentrations as low as 1 mM. Ca2+, Zn2+, Fe2+ and Cd2+ could not replace Mg2+ either, instead they inhibited Succinyl CoA Synthetase. 3. 3. The assay with the monovalent cations chlorides K +, NH+ 4, Na+ and Li+ showed that maximum activation for the first three was found at 50-60 mM while Li+ had no effect. Increasing concentrations of these cations progressivey progressively inhibited enzyme activity. © 1980.
format JOUR
author De Xifra, E.A.W.
Del C. Batlle, A.M.
author_facet De Xifra, E.A.W.
Del C. Batlle, A.M.
author_sort De Xifra, E.A.W.
title Porphyrin biosynthesis in the soybean callus system-XVII. Effect of monovalent and divalent cations on the activity of succinyl CoA synthetase
title_short Porphyrin biosynthesis in the soybean callus system-XVII. Effect of monovalent and divalent cations on the activity of succinyl CoA synthetase
title_full Porphyrin biosynthesis in the soybean callus system-XVII. Effect of monovalent and divalent cations on the activity of succinyl CoA synthetase
title_fullStr Porphyrin biosynthesis in the soybean callus system-XVII. Effect of monovalent and divalent cations on the activity of succinyl CoA synthetase
title_full_unstemmed Porphyrin biosynthesis in the soybean callus system-XVII. Effect of monovalent and divalent cations on the activity of succinyl CoA synthetase
title_sort porphyrin biosynthesis in the soybean callus system-xvii. effect of monovalent and divalent cations on the activity of succinyl coa synthetase
url http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p717_DeXifra
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