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...
Guardado en:
| Publicado: |
1988
|
|---|---|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v20_n7_p703_Goldemberg http://hdl.handle.net/20.500.12110/paper_0020711X_v20_n7_p703_Goldemberg |
| Aporte de: |
| id |
paper:paper_0020711X_v20_n7_p703_Goldemberg |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_0020711X_v20_n7_p703_Goldemberg2023-06-08T14:41:09Z Allosteric transition of erythrocyte alkaline phosphatase from duchenne muscular dystrophy (DMD) patients and duchenne muscular dystrophy carriers (Homo sapiens) 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. 1988 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v20_n7_p703_Goldemberg 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 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. |
| 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) |
| publishDate |
1988 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v20_n7_p703_Goldemberg http://hdl.handle.net/20.500.12110/paper_0020711X_v20_n7_p703_Goldemberg |
| _version_ |
1768541548576768000 |