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spelling paper:paper_00145793_v27_n2_p275_deXifra2023-06-08T14:37:34Z Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support Batlle, Alcira María del Carmen adenosine triphosphate long chain fatty acid coenzyme A ligase polysaccharide succinic acid derivative affinity chromatography article binding site enzymology kinetics macromolecule metabolism plant protein binding Adenosine Triphosphate Binding Sites Chromatography, Affinity Coenzyme A Ligases Kinetics Macromolecular Systems Plants Polysaccharides Protein Binding Succinates Fil:del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1972 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v27_n2_p275_deXifra http://hdl.handle.net/20.500.12110/paper_00145793_v27_n2_p275_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 adenosine triphosphate
long chain fatty acid coenzyme A ligase
polysaccharide
succinic acid derivative
affinity chromatography
article
binding site
enzymology
kinetics
macromolecule
metabolism
plant
protein binding
Adenosine Triphosphate
Binding Sites
Chromatography, Affinity
Coenzyme A Ligases
Kinetics
Macromolecular Systems
Plants
Polysaccharides
Protein Binding
Succinates
spellingShingle adenosine triphosphate
long chain fatty acid coenzyme A ligase
polysaccharide
succinic acid derivative
affinity chromatography
article
binding site
enzymology
kinetics
macromolecule
metabolism
plant
protein binding
Adenosine Triphosphate
Binding Sites
Chromatography, Affinity
Coenzyme A Ligases
Kinetics
Macromolecular Systems
Plants
Polysaccharides
Protein Binding
Succinates
Batlle, Alcira María del Carmen
Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support
topic_facet adenosine triphosphate
long chain fatty acid coenzyme A ligase
polysaccharide
succinic acid derivative
affinity chromatography
article
binding site
enzymology
kinetics
macromolecule
metabolism
plant
protein binding
Adenosine Triphosphate
Binding Sites
Chromatography, Affinity
Coenzyme A Ligases
Kinetics
Macromolecular Systems
Plants
Polysaccharides
Protein Binding
Succinates
description Fil:del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
author Batlle, Alcira María del Carmen
author_facet Batlle, Alcira María del Carmen
author_sort Batlle, Alcira María del Carmen
title Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support
title_short Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support
title_full Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support
title_fullStr Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support
title_full_unstemmed Studies on the reaction mechanism of soybean callus succinyl CoA synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support
title_sort studies on the reaction mechanism of soybean callus succinyl coa synthetase. phosphorylation of the enzyme on immobilized adenosine-triphosphate and enzyme attached to a solid support
publishDate 1972
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v27_n2_p275_deXifra
http://hdl.handle.net/20.500.12110/paper_00145793_v27_n2_p275_deXifra
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