In vitro effect of cyanide, thiosulphate and S-adenosyl-l-methionine on the activity of rhodanese and other enzymes

1. 1. Some in vitro studies were performed to elucidate the action of S-adenosyl-l-methionine (SAM) and thiosulphate on liver rhodanese, δ-amino-levulinic acid dehydratase (ALA-D) and cytochrome oxidase affected by cyanide in the experimental conditions. 2. 2. SAM was unable to interact with the sul...

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Detalles Bibliográficos
Autor principal: Buzaleh, A.M
Otros Autores: Vazquez, E.S, Del Carmen Batlle, A.M
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1991
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
Aporte de:Registro referencial: Solicitar el recurso aquí
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024 7 |2 scopus  |a 2-s2.0-0025966801 
024 7 |2 cas  |a cyanide, 57-12-5; cytochrome c oxidase, 72841-18-0, 9001-16-5; porphobilinogen synthase, 9036-37-7; s adenosylmethionine, 29908-03-0, 485-80-3; thiosulfate sulfurtransferase, 9026-04-4; thiosulfate, 14383-50-7; Cyanides; Cytochrome-c Oxidase, EC 1.9.3.1; Porphobilinogen Synthase, EC 4.2.1.24; S-Adenosylmethionine, 29908-03-0; Thiosulfate Sulfurtransferase, EC 2.8.1.1; Thiosulfates 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a GEPHD 
100 1 |a Buzaleh, A.M. 
245 1 3 |a In vitro effect of cyanide, thiosulphate and S-adenosyl-l-methionine on the activity of rhodanese and other enzymes 
260 |c 1991 
270 1 0 |m Del Carmen Batlle, A.M.; Centro de Investigaciones sobre Profirinas, Porfirias (CIPYP)-CONICET-Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires (UBA), Calle Viamonte 444/, 430 Buenos Aires, Argentina 
506 |2 openaire  |e Política editorial 
504 |a Antonini, Brunori, Greenwood, Malmström, Rotilio, The interaction of cyanide with cytochrome oxidase (1971) Eur. J. Biochem., 23, pp. 396-400 
504 |a Batlle, Ferramola, Grinstein, Purification and general properties of δ-aminolaevulate dehydratase for cow liver (1967) Biochem. J., 104, pp. 244-249 
504 |a Burnham, Lascelles, Control of porphyrin biosynthesis through a negative-feedback mechanism: Studies with preparations of δ-aminolaevulate synthetase and δ-aminolaevulic dehydratase from Rp (1963) spheroides. Biochem. J., 87, pp. 462-472 
504 |a Buzaleh, Vázquez, Batlle, Cyanide intoxication III: on the analogous and different effects provoked by non-lethal and lethal challenge doses (1990) Gen. Pharmac., 21, pp. 27-32 
504 |a Davidson, Westley, Tryptophan in the active site of rhodanese (1965) J. Biol. Chem., 240, pp. 4463-4469 
504 |a De Toma, Westley, Effect of sulphur binding on rhodanese fluorescence (1970) Biochimica et Biophysica Acta (BBA) - Protein Structure, 207, pp. 144-149 
504 |a Gibson, Neuberger, Scott, The purification and properties of δ-aminolevulinic acid dehydratase (1955) Biochem. J., 61, pp. 618-629 
504 |a Hill, Robinson, Cyanide binding to bovine heart cytochrome c coxidase depleted of subunit III by treatment with lauryl maltoside (1986) J. Biol. Chem., 261, pp. 15356-15359 
504 |a Lowry, Rosebrough, Farr, Randall, Protein measurement with the Folin-Phenol reagent (1951) J. Biol. Chem., 193, pp. 265-275 
504 |a Nandi, Baker-Cohen, Shemin, δ-Aminolevulinic acid dehydratase of Rp. spheroides I Isolation and mechanism (1968) J. Biol. Chem., 243, pp. 1224-1230 
504 |a Paredes, Kozicki, Batlle, S-Adenosyl-l-methionine a counter to lead intoxication? (1985) Comp. Biochem. Physiol., 82 B, pp. 751-757 
504 |a Schubert, Brill, Antagonism of experimental cyanide toxicity in relation to the in vivo activity of cytochrome oxidase (1968) J. Pharmac. Exp. Ther., 162, pp. 352-359 
504 |a Shemin, δ-Aminolaevulinic-Dehydratase; structure, function and mechanism (1976) Phil. Trans. R. Soc. Lond. B, 273, pp. 109-115 
504 |a Solomonson, Cyanide as metabolic inhibitor (1982) Cyanide in Biology, pp. 11-28. , B. Vennsland, E.E. Conn, C.J. Knowles, J. Westley, F. Wissing, Academic Press, London 
504 |a Sommer, Beyersmann, Zinc and cadmium in 5-aminoleuvulinic acid dehydratase (1984) Equilibrium, kinetic and 113Cd-nmr-studies, 20, pp. 131-145. , J. Inorgan. Biochem 
504 |a Sörbo, Rhodanese (1955) Methods in Enzymology, 11, pp. 334-335. , S.P. Collowick, N.O. Kaplan, Academic Press, New York 
504 |a Sörbo, Enzymatic conversion of cyanide to thiocyanate (1962) The Proceedings of the First International Pharmacological Meeting 6: Metabolic Factors Controlling Duration of Drug Action, pp. 121-128. , B.B. Brodie, E.G. Erdos, MacMillan, New York 
504 |a Van Buuren, Nicholls, van Gelder, Biochemical and biophysical studies on cytochrome aa3 VI. Reaction of cyanide with oxidized and reduced enzyme (1972) Biochim. Biophys. Acta, 256, pp. 258-276 
504 |a Vázquez, Investigación de los niveles de enzimas relacionadas con la biosíntesis de tetrapirroles en modelos vegetales y en individuos normales y porfiricos (1984) Doctoral Thesis, pp. 290-299. , University of Buenos Aires 
504 |a Wang, Volini, Studies on the active site of rhodanese (1968) J. Biol. Chem., 243, pp. 5465-5470 
504 |a Way, Gibbons, Sheehy, Effect of oxygen on cyanide intoxication I. Prophylactic protection (1966) J. Pharmac. Exp. Ther., 153, pp. 351-355 
504 |a Westley, Rhodanese and the sulfane pool (1980) Enzymatic Basis of Detoxification. Biochemical Pharmacology and Toxicology. A series of Monographs, 2, pp. 245-262. , W.B. Jakoby, Academic Press, New York, Chapter 13 
504 |a Westley, Rhodanese (1981) Methods in Enzymology, 77, pp. 285-291. , S.P. Collowick, N.O. Nathan, Academic Press, New York 
504 |a Yonetani, Ray, Studies on cytochrome oxidase VI. Kinetics of the aerobic oxidation of ferrocytochrome c by cytochrome oxidase (1965) J. Biol. Chem., 240, pp. 3392-3398 
520 3 |a 1. 1. Some in vitro studies were performed to elucidate the action of S-adenosyl-l-methionine (SAM) and thiosulphate on liver rhodanese, δ-amino-levulinic acid dehydratase (ALA-D) and cytochrome oxidase affected by cyanide in the experimental conditions. 2. 2. SAM was unable to interact with the sulfur substituted rhodanese complex suggesting that SAM would blockade the thiosulphate binding sites on rhodanese. 3. 3. Cyanide and thiosulphate inhibited ALA-D activity when both compounds were present in the incubation or the preincubation mixture. Cyanide binding on the enzyme was irreversible. 4. 4. Cyanide inhibited cytochrome oxidase activity and the reversible nature of the binding was demonstrated by gel filtration. 5. 5. SAM had no effect on either ALA-D or cytochrome oxidase activities. © 1991.  |l eng 
536 |a Detalles de la financiación: Universidad de Buenos Aires 
536 |a Detalles de la financiación: Ministerio de la Producción, Ciencia y Tecnología, MEC 
536 |a Detalles de la financiación: Secretaria de Ciencia y Tecnica, Universidad de Buenos Aires 
536 |a Detalles de la financiación: Association for International Cancer Research 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: Acknowledgements--A. M. del C. Batlle holds the post of Superior Scientific Researcher in the Argentine National Research Council (CONICET); E. Vfizquez and A. M. Buzaleh are Research Fellows at the CONICET. This work was supported by grants from the CONICET, the SECYT, UBA and Banco de la Naci6n Argentina. We wish to express our gratitude to Lic. S. Afonso for the excellent drawings. A. M. C. Batlle thanks the Ministerio de Educa-ci6n y Ciencia (MEC) of Spain and the Association for International Cancer Research (AICR)-UK for special help. 
593 |a Centro de Investigaciones sobre Profirinas, Porfirias (CIPYP)-CONICET-Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires (UBA), Calle Viamonte 444/, 430 Buenos Aires, Argentina 
690 1 0 |a CYANIDE 
690 1 0 |a CYTOCHROME C OXIDASE 
690 1 0 |a PORPHOBILINOGEN SYNTHASE 
690 1 0 |a S ADENOSYLMETHIONINE 
690 1 0 |a THIOSULFATE 
690 1 0 |a THIOSULFATE SULFURTRANSFERASE 
690 1 0 |a ANIMAL TISSUE 
690 1 0 |a ARTICLE 
690 1 0 |a CONTROLLED STUDY 
690 1 0 |a ENZYME ACTIVITY 
690 1 0 |a LIVER HOMOGENATE 
690 1 0 |a MOUSE 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a ANIMAL 
690 1 0 |a CYANIDES 
690 1 0 |a CYTOCHROME-C OXIDASE 
690 1 0 |a IN VITRO 
690 1 0 |a LIVER 
690 1 0 |a MICE 
690 1 0 |a PORPHOBILINOGEN SYNTHASE 
690 1 0 |a S-ADENOSYLMETHIONINE 
690 1 0 |a SUPPORT, NON-U.S. GOV'T 
690 1 0 |a THIOSULFATE SULFURTRANSFERASE 
690 1 0 |a THIOSULFATES 
700 1 |a Vazquez, E.S. 
700 1 |a Del Carmen Batlle, A.M. 
773 0 |d 1991  |g v. 22  |h pp. 281-286  |k n. 2  |p Gen. Pharmacol. Vasc. Syst.  |x 03063623  |w (AR-BaUEN)CENRE-4808  |t General Pharmacology 
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