Reduced thiosulphate affinity for erythrocyte rhodanese: An explanation for increased δ-aminolevulinic synthetase activity in some porphyrias?

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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 studi...

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Detalles Bibliográficos
Autor principal: Vazquez, E.
Otros Autores: Buzaleh, A.M, Wider, E., Batlle, A.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1986
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
Aporte de:Registro referencial: Solicitar el recurso aquí
Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 scopus  |a 2-s2.0-0023008862 
024 7 |2 cas  |a 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 
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100 1 |a Vazquez, E. 
245 1 0 |a Reduced thiosulphate affinity for erythrocyte rhodanese: An explanation for increased δ-aminolevulinic synthetase activity in some porphyrias? 
260 |c 1986 
506 |2 openaire  |e Política editorial 
520 3 |a 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.  |l eng 
593 |a Centro de Investigaciones sobre Porfirinas y Porfirias (CIPYP) (FCEN, UBA-CONICET), Ciudad Universitaria, Pabellon II, 1428 Buenos Aires, Argentina 
690 1 0 |a 5 AMINOLEVULINATE SYNTHASE 
690 1 0 |a CYSTINE 
690 1 0 |a THIOCYANIC ACID 
690 1 0 |a THIOSULFATE 
690 1 0 |a THIOSULFATE SULFURTRANSFERASE 
690 1 0 |a UNCLASSIFIED DRUG 
690 1 0 |a BLOOD AND HEMOPOIETIC SYSTEM 
690 1 0 |a CHROMATOGRAPHY 
690 1 0 |a CYTOCHEMISTRY 
690 1 0 |a CYTOLOGY 
690 1 0 |a DRUG EFFICACY 
690 1 0 |a ERYTHROCYTE 
690 1 0 |a HUMAN 
690 1 0 |a HUMAN CELL 
690 1 0 |a PORPHYRIA 
690 1 0 |a PRIORITY JOURNAL 
700 1 |a Buzaleh, A.M. 
700 1 |a Wider, E. 
700 1 |a Batlle, A. 
773 0 |d 1986  |g v. 14  |h pp. 999-1000  |k n. 10  |p IRCS MED. SCI.  |x 03056651  |t IRCS Medical Science 
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856 4 0 |u https://hdl.handle.net/20.500.12110/paper_03056651_v14_n10_p999_Vazquez  |y Handle 
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962 |a info:eu-repo/semantics/article  |a info:ar-repo/semantics/artículo  |b info:eu-repo/semantics/publishedVersion 
999 |c 61898 

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