Artículo
Abstract:
Rhodanese from normal individuals' and acute intermittent porphyria (AIP) patients' red blood cells (RBC) was purified 134-fold, with a final yield of 20%. Normal and AIP RBC rhodanese exhibited practically the same chromatographic behaviour and also an optimum pH around 9.3. Kinetic studies from normal RBC rhodanese showed substrate inhibition at high thiosulphate and cyanide concentration, while results obtained for the AIP RBC rhodanese showed substrate inhibition at high cyanide concentrations, but no inhibition at high thiosulphate concentration. Vmax and Km were similar for normal and AIP rhodanese when cyanide was the variable substrate, but those parameters differed when thiosulphate varied. On the basis of these findings it is postulated that in AIP, as a consequence of reduced affinity of rhodanese for thiosulphate, cystine trisulphide, the ALA-S activator and sulphur donor substrate for rhodanese, would not be acted on or degraded, remaining in higher concentrations than normal. As a result the activity of ALA-S would be increased, failing to operate the rhodanese control mechanism.
Registro:
| Documento: | Artículo |
| Título: | Reduced thiosulphate affinity for erythrocyte rhodanese: An explanation for increased δ-aminolevulinic synthetase activity in some porphyrias? |
| Autor: | Vazquez, E.; Buzaleh, A.M.; Wider, E.; Batlle, A. |
| Filiación: | Centro de Investigaciones sobre Porfirinas y Porfirias (CIPYP) (FCEN, UBA-CONICET), Ciudad Universitaria, Pabellon II, 1428 Buenos Aires, Argentina |
| Palabras clave: | 5 aminolevulinate synthase; cystine; thiocyanic acid; thiosulfate; thiosulfate sulfurtransferase; unclassified drug; blood and hemopoietic system; chromatography; cytochemistry; cytology; drug efficacy; erythrocyte; human; human cell; porphyria; priority journal |
| Año: | 1986 |
| Volumen: | 14 |
| Número: | 10 |
| Página de inicio: | 999 |
| Página de fin: | 1000 |
| Título revista: | IRCS Medical Science |
| Título revista abreviado: | IRCS MED. SCI. |
| ISSN: | 03056651 |
| CODEN: | IRLCD |
| CAS: | 5 aminolevulinate synthase, 9037-14-3; cystine, 24645-67-8, 56-89-3, 6020-39-9; thiosulfate, 14383-50-7; thiosulfate sulfurtransferase, 9026-04-4 |
| Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03056651_v14_n10_p999_Vazquez |
Citas:
---------- APA ----------
Vazquez, E., Buzaleh, A.M., Wider, E. & Batlle, A. (1986) . Reduced thiosulphate affinity for erythrocyte rhodanese: An explanation for increased δ-aminolevulinic synthetase activity in some porphyrias?. IRCS Medical Science, 14(10), 999-1000.Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03056651_v14_n10_p999_Vazquez [ ]
---------- CHICAGO ----------
Vazquez, E., Buzaleh, A.M., Wider, E., Batlle, A. "Reduced thiosulphate affinity for erythrocyte rhodanese: An explanation for increased δ-aminolevulinic synthetase activity in some porphyrias?" . IRCS Medical Science 14, no. 10 (1986) : 999-1000.Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03056651_v14_n10_p999_Vazquez [ ]
---------- MLA ----------
Vazquez, E., Buzaleh, A.M., Wider, E., Batlle, A. "Reduced thiosulphate affinity for erythrocyte rhodanese: An explanation for increased δ-aminolevulinic synthetase activity in some porphyrias?" . IRCS Medical Science, vol. 14, no. 10, 1986, pp. 999-1000.Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03056651_v14_n10_p999_Vazquez [ ]
---------- VANCOUVER ----------
Vazquez, E., Buzaleh, A.M., Wider, E., Batlle, A. Reduced thiosulphate affinity for erythrocyte rhodanese: An explanation for increased δ-aminolevulinic synthetase activity in some porphyrias?. IRCS MED. SCI. 1986;14(10):999-1000.Available from: https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03056651_v14_n10_p999_Vazquez [ ]
