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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Autor principal: Batlle, Alcira María del Carmen
Publicado: 1980
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v12_n5-6_p717_DeXifra
http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p717_DeXifra
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spelling paper:paper_0020711X_v12_n5-6_p717_DeXifra2023-06-08T14:41:02Z Porphyrin biosynthesis in the soybean callus system-XVII. Effect of monovalent and divalent cations on the activity of succinyl CoA synthetase Batlle, Alcira María del Carmen 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. 1980 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v12_n5-6_p717_DeXifra 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
Batlle, Alcira María del Carmen
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.
author Batlle, Alcira María del Carmen
author_facet Batlle, Alcira María del Carmen
author_sort Batlle, Alcira María del Carmen
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
publishDate 1980
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v12_n5-6_p717_DeXifra
http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p717_DeXifra
work_keys_str_mv AT batllealciramariadelcarmen porphyrinbiosynthesisinthesoybeancallussystemxviieffectofmonovalentanddivalentcationsontheactivityofsuccinylcoasynthetase
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