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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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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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 |
_version_ |
1768543687374012416 |