Acyl-CoA synthetase activity in liver microsomes from calcium-deficient rats

Autores
Marra, Carlos Alberto; Tacconi de Alaniz, María Josefa
Año de publicación
1999
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A study on the kinetic properties of the nonspecific acyl-coenzyme A (CoA) synthetase activity in liver microsomal vesicles from both normal and calcium-deficient Wistar rats was carried out. After a 65-d treatment, the calcium-deficient diet reflected a 75% increase in the synthetase activity with respect to control animals. The apparent Vm was significantly enhanced, while the Km remained unchanged. We also provided experimental evidence about various fatty acids of different carbon length and unsaturation which depressed the biosynthesis of palmitoyl-CoA following different behaviors in control or calcium-deprived liver microsomes. In addition, we studied in detail the inhibition reflected by stearic, α-linolenic, or arachidonic acids, in the biosynthesis of palmitoyl-CoA in microsomal suspensions either from control or hypocalcemic rats. In control microsomes, stearic acid produced a pure competitive effect, while the other fatty acids followed a mixed-type inhibition. The competitive effect of stearic acid was not observed in calcium-deprived microsomes. At the same time, a mixed-type inhibition produced by either α-linolenic or arachidonic acid was diminished in deprived microsomes due to an increase in the noncompetitive component (αKi). These changes observed in apparent kinetic constants (Km, Vm, Ki, and αKi), as determined by Lineweaver-Burks and Dixon plots, were attributed to the important alterations in the physicochemical properties of the endoplasmic reticulum membranes induced by the calcium-deficient diet. The solubilization of the enzyme activity from both types of microsomes demonstrated that the kinetic behavior of the enzyme depends on the microenvironment in the membrane, and that the calcium ion plays a crucial role in determining the alterations observed.
Instituto de Investigaciones Bioquímicas de La Plata
Materia
Biología
Acyl-coenzyme A
Kinetic properties
Calcium-deficient diet
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-nd/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/146380

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spelling Acyl-CoA synthetase activity in liver microsomes from calcium-deficient ratsMarra, Carlos AlbertoTacconi de Alaniz, María JosefaBiologíaAcyl-coenzyme AKinetic propertiesCalcium-deficient dietA study on the kinetic properties of the nonspecific acyl-coenzyme A (CoA) synthetase activity in liver microsomal vesicles from both normal and calcium-deficient Wistar rats was carried out. After a 65-d treatment, the calcium-deficient diet reflected a 75% increase in the synthetase activity with respect to control animals. The apparent Vm was significantly enhanced, while the Km remained unchanged. We also provided experimental evidence about various fatty acids of different carbon length and unsaturation which depressed the biosynthesis of palmitoyl-CoA following different behaviors in control or calcium-deprived liver microsomes. In addition, we studied in detail the inhibition reflected by stearic, α-linolenic, or arachidonic acids, in the biosynthesis of palmitoyl-CoA in microsomal suspensions either from control or hypocalcemic rats. In control microsomes, stearic acid produced a pure competitive effect, while the other fatty acids followed a mixed-type inhibition. The competitive effect of stearic acid was not observed in calcium-deprived microsomes. At the same time, a mixed-type inhibition produced by either α-linolenic or arachidonic acid was diminished in deprived microsomes due to an increase in the noncompetitive component (αKi). These changes observed in apparent kinetic constants (Km, Vm, Ki, and αKi), as determined by Lineweaver-Burks and Dixon plots, were attributed to the important alterations in the physicochemical properties of the endoplasmic reticulum membranes induced by the calcium-deficient diet. The solubilization of the enzyme activity from both types of microsomes demonstrated that the kinetic behavior of the enzyme depends on the microenvironment in the membrane, and that the calcium ion plays a crucial role in determining the alterations observed.Instituto de Investigaciones Bioquímicas de La Plata1999info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf343-354http://sedici.unlp.edu.ar/handle/10915/146380enginfo:eu-repo/semantics/altIdentifier/issn/0024-4201info:eu-repo/semantics/altIdentifier/issn/1558-9307info:eu-repo/semantics/altIdentifier/doi/10.1007/s11745-999-0372-xinfo:eu-repo/semantics/altIdentifier/pmid/10443967info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/4.0/Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:32:36Zoai:sedici.unlp.edu.ar:10915/146380Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:32:36.918SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Acyl-CoA synthetase activity in liver microsomes from calcium-deficient rats
title Acyl-CoA synthetase activity in liver microsomes from calcium-deficient rats
spellingShingle Acyl-CoA synthetase activity in liver microsomes from calcium-deficient rats
Marra, Carlos Alberto
Biología
Acyl-coenzyme A
Kinetic properties
Calcium-deficient diet
title_short Acyl-CoA synthetase activity in liver microsomes from calcium-deficient rats
title_full Acyl-CoA synthetase activity in liver microsomes from calcium-deficient rats
title_fullStr Acyl-CoA synthetase activity in liver microsomes from calcium-deficient rats
title_full_unstemmed Acyl-CoA synthetase activity in liver microsomes from calcium-deficient rats
title_sort Acyl-CoA synthetase activity in liver microsomes from calcium-deficient rats
dc.creator.none.fl_str_mv Marra, Carlos Alberto
Tacconi de Alaniz, María Josefa
author Marra, Carlos Alberto
author_facet Marra, Carlos Alberto
Tacconi de Alaniz, María Josefa
author_role author
author2 Tacconi de Alaniz, María Josefa
author2_role author
dc.subject.none.fl_str_mv Biología
Acyl-coenzyme A
Kinetic properties
Calcium-deficient diet
topic Biología
Acyl-coenzyme A
Kinetic properties
Calcium-deficient diet
dc.description.none.fl_txt_mv A study on the kinetic properties of the nonspecific acyl-coenzyme A (CoA) synthetase activity in liver microsomal vesicles from both normal and calcium-deficient Wistar rats was carried out. After a 65-d treatment, the calcium-deficient diet reflected a 75% increase in the synthetase activity with respect to control animals. The apparent Vm was significantly enhanced, while the Km remained unchanged. We also provided experimental evidence about various fatty acids of different carbon length and unsaturation which depressed the biosynthesis of palmitoyl-CoA following different behaviors in control or calcium-deprived liver microsomes. In addition, we studied in detail the inhibition reflected by stearic, α-linolenic, or arachidonic acids, in the biosynthesis of palmitoyl-CoA in microsomal suspensions either from control or hypocalcemic rats. In control microsomes, stearic acid produced a pure competitive effect, while the other fatty acids followed a mixed-type inhibition. The competitive effect of stearic acid was not observed in calcium-deprived microsomes. At the same time, a mixed-type inhibition produced by either α-linolenic or arachidonic acid was diminished in deprived microsomes due to an increase in the noncompetitive component (αKi). These changes observed in apparent kinetic constants (Km, Vm, Ki, and αKi), as determined by Lineweaver-Burks and Dixon plots, were attributed to the important alterations in the physicochemical properties of the endoplasmic reticulum membranes induced by the calcium-deficient diet. The solubilization of the enzyme activity from both types of microsomes demonstrated that the kinetic behavior of the enzyme depends on the microenvironment in the membrane, and that the calcium ion plays a crucial role in determining the alterations observed.
Instituto de Investigaciones Bioquímicas de La Plata
description A study on the kinetic properties of the nonspecific acyl-coenzyme A (CoA) synthetase activity in liver microsomal vesicles from both normal and calcium-deficient Wistar rats was carried out. After a 65-d treatment, the calcium-deficient diet reflected a 75% increase in the synthetase activity with respect to control animals. The apparent Vm was significantly enhanced, while the Km remained unchanged. We also provided experimental evidence about various fatty acids of different carbon length and unsaturation which depressed the biosynthesis of palmitoyl-CoA following different behaviors in control or calcium-deprived liver microsomes. In addition, we studied in detail the inhibition reflected by stearic, α-linolenic, or arachidonic acids, in the biosynthesis of palmitoyl-CoA in microsomal suspensions either from control or hypocalcemic rats. In control microsomes, stearic acid produced a pure competitive effect, while the other fatty acids followed a mixed-type inhibition. The competitive effect of stearic acid was not observed in calcium-deprived microsomes. At the same time, a mixed-type inhibition produced by either α-linolenic or arachidonic acid was diminished in deprived microsomes due to an increase in the noncompetitive component (αKi). These changes observed in apparent kinetic constants (Km, Vm, Ki, and αKi), as determined by Lineweaver-Burks and Dixon plots, were attributed to the important alterations in the physicochemical properties of the endoplasmic reticulum membranes induced by the calcium-deficient diet. The solubilization of the enzyme activity from both types of microsomes demonstrated that the kinetic behavior of the enzyme depends on the microenvironment in the membrane, and that the calcium ion plays a crucial role in determining the alterations observed.
publishDate 1999
dc.date.none.fl_str_mv 1999
dc.type.none.fl_str_mv info:eu-repo/semantics/article
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Articulo
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info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/146380
url http://sedici.unlp.edu.ar/handle/10915/146380
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info:eu-repo/semantics/altIdentifier/issn/1558-9307
info:eu-repo/semantics/altIdentifier/doi/10.1007/s11745-999-0372-x
info:eu-repo/semantics/altIdentifier/pmid/10443967
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-nd/4.0/
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
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rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/4.0/
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