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

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...

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Autores principales: Marra, Carlos Alberto, Tacconi de Alaniz, María Josefa
Formato: Articulo
Lenguaje:Inglés
Publicado: 1999
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Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/146380
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id I19-R120-10915-146380
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
Acyl-coenzyme A
Kinetic properties
Calcium-deficient diet
spellingShingle Biología
Acyl-coenzyme A
Kinetic properties
Calcium-deficient diet
Marra, Carlos Alberto
Tacconi de Alaniz, María Josefa
Acyl-CoA synthetase activity in liver microsomes from calcium-deficient rats
topic_facet Biología
Acyl-coenzyme A
Kinetic properties
Calcium-deficient diet
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.
format Articulo
Articulo
author Marra, Carlos Alberto
Tacconi de Alaniz, María Josefa
author_facet Marra, Carlos Alberto
Tacconi de Alaniz, María Josefa
author_sort Marra, Carlos Alberto
title Acyl-CoA synthetase activity in liver microsomes from calcium-deficient rats
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
publishDate 1999
url http://sedici.unlp.edu.ar/handle/10915/146380
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AT tacconidealanizmariajosefa acylcoasynthetaseactivityinlivermicrosomesfromcalciumdeficientrats
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