Allosteric transition of erythrocyte alkaline phosphatase from duchenne muscular dystrophy (DMD) patients and duchenne muscular dystrophy carriers (Homo sapiens)

1. 1. The kinetic properties of the p-nitrophenylphosphatase (EC 3.1.3.1) from erythrocytes was investigated in DMD-patients and DMD-carriers. 2. 2. A different allosteric behaviour in the p-nitrophenylphosphatase from DMD-patients and DMD-carriers compared to controls is supported by the following...

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Autores principales: Goldemberg, A.L., García, A.M., Fernández, H., Fortunato, M., Sánchez, J.J., Trucco, R.E.
Formato: JOUR
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0020711X_v20_n7_p703_Goldemberg
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spelling todo:paper_0020711X_v20_n7_p703_Goldemberg2023-10-03T14:17:59Z Allosteric transition of erythrocyte alkaline phosphatase from duchenne muscular dystrophy (DMD) patients and duchenne muscular dystrophy carriers (Homo sapiens) Goldemberg, A.L. García, A.M. Fernández, H. Fortunato, M. Sánchez, J.J. Trucco, R.E. alkaline phosphatase allosterism case report duchenne muscular dystrophy erythrocyte heterozygote human human cell 4-Nitrophenylphosphatase Alkaline Phosphatase Allosteric Regulation Erythrocyte Membrane Female Fluorides Heterozygote Human In Vitro Kinetics Magnesium Male Muscular Dystrophies Phosphoric Monoester Hydrolases Support, Non-U.S. Gov't 1. 1. The kinetic properties of the p-nitrophenylphosphatase (EC 3.1.3.1) from erythrocytes was investigated in DMD-patients and DMD-carriers. 2. 2. A different allosteric behaviour in the p-nitrophenylphosphatase from DMD-patients and DMD-carriers compared to controls is supported by the following finclings: (a) values of n altered in F- inhibition of (K+-activated p-nitrophenylphosphatase with Hill coefficients -1.5, -2.2 and -3.1; (b) heterotropic effect of increased concentration of Mg2+ on F- inhibition which is reverted by K+ in DMD-carriers and in control, but not in DMD-patients. 3. 3. Evidence is presented showing that in DMD-patients and in DMD-carriers the interaction membrane-enzyme is different from the corresponcling controls. © 1988. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0020711X_v20_n7_p703_Goldemberg
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic alkaline phosphatase
allosterism
case report
duchenne muscular dystrophy
erythrocyte
heterozygote
human
human cell
4-Nitrophenylphosphatase
Alkaline Phosphatase
Allosteric Regulation
Erythrocyte Membrane
Female
Fluorides
Heterozygote
Human
In Vitro
Kinetics
Magnesium
Male
Muscular Dystrophies
Phosphoric Monoester Hydrolases
Support, Non-U.S. Gov't
spellingShingle alkaline phosphatase
allosterism
case report
duchenne muscular dystrophy
erythrocyte
heterozygote
human
human cell
4-Nitrophenylphosphatase
Alkaline Phosphatase
Allosteric Regulation
Erythrocyte Membrane
Female
Fluorides
Heterozygote
Human
In Vitro
Kinetics
Magnesium
Male
Muscular Dystrophies
Phosphoric Monoester Hydrolases
Support, Non-U.S. Gov't
Goldemberg, A.L.
García, A.M.
Fernández, H.
Fortunato, M.
Sánchez, J.J.
Trucco, R.E.
Allosteric transition of erythrocyte alkaline phosphatase from duchenne muscular dystrophy (DMD) patients and duchenne muscular dystrophy carriers (Homo sapiens)
topic_facet alkaline phosphatase
allosterism
case report
duchenne muscular dystrophy
erythrocyte
heterozygote
human
human cell
4-Nitrophenylphosphatase
Alkaline Phosphatase
Allosteric Regulation
Erythrocyte Membrane
Female
Fluorides
Heterozygote
Human
In Vitro
Kinetics
Magnesium
Male
Muscular Dystrophies
Phosphoric Monoester Hydrolases
Support, Non-U.S. Gov't
description 1. 1. The kinetic properties of the p-nitrophenylphosphatase (EC 3.1.3.1) from erythrocytes was investigated in DMD-patients and DMD-carriers. 2. 2. A different allosteric behaviour in the p-nitrophenylphosphatase from DMD-patients and DMD-carriers compared to controls is supported by the following finclings: (a) values of n altered in F- inhibition of (K+-activated p-nitrophenylphosphatase with Hill coefficients -1.5, -2.2 and -3.1; (b) heterotropic effect of increased concentration of Mg2+ on F- inhibition which is reverted by K+ in DMD-carriers and in control, but not in DMD-patients. 3. 3. Evidence is presented showing that in DMD-patients and in DMD-carriers the interaction membrane-enzyme is different from the corresponcling controls. © 1988.
format JOUR
author Goldemberg, A.L.
García, A.M.
Fernández, H.
Fortunato, M.
Sánchez, J.J.
Trucco, R.E.
author_facet Goldemberg, A.L.
García, A.M.
Fernández, H.
Fortunato, M.
Sánchez, J.J.
Trucco, R.E.
author_sort Goldemberg, A.L.
title Allosteric transition of erythrocyte alkaline phosphatase from duchenne muscular dystrophy (DMD) patients and duchenne muscular dystrophy carriers (Homo sapiens)
title_short Allosteric transition of erythrocyte alkaline phosphatase from duchenne muscular dystrophy (DMD) patients and duchenne muscular dystrophy carriers (Homo sapiens)
title_full Allosteric transition of erythrocyte alkaline phosphatase from duchenne muscular dystrophy (DMD) patients and duchenne muscular dystrophy carriers (Homo sapiens)
title_fullStr Allosteric transition of erythrocyte alkaline phosphatase from duchenne muscular dystrophy (DMD) patients and duchenne muscular dystrophy carriers (Homo sapiens)
title_full_unstemmed Allosteric transition of erythrocyte alkaline phosphatase from duchenne muscular dystrophy (DMD) patients and duchenne muscular dystrophy carriers (Homo sapiens)
title_sort allosteric transition of erythrocyte alkaline phosphatase from duchenne muscular dystrophy (dmd) patients and duchenne muscular dystrophy carriers (homo sapiens)
url http://hdl.handle.net/20.500.12110/paper_0020711X_v20_n7_p703_Goldemberg
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