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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Detalles Bibliográficos
Autores principales: Goldemberg, A.L., García, A.M., Fernández, H., Fortunato, M., Sánchez, J.J., Trucco, R.E.
Formato: JOUR
Materias:
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
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0020711X_v20_n7_p703_Goldemberg
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario: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.

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