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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Autores principales: Buzaleh, Ana María, Vázquez, Elba Susana, Batlle, Alcira María del Carmen
Publicado: 1991
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03063623_v22_n2_p281_Buzaleh
http://hdl.handle.net/20.500.12110/paper_03063623_v22_n2_p281_Buzaleh
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spelling paper:paper_03063623_v22_n2_p281_Buzaleh2023-06-08T15:31:05Z In vitro effect of cyanide, thiosulphate and S-adenosyl-l-methionine on the activity of rhodanese and other enzymes Buzaleh, Ana María Vázquez, Elba Susana Batlle, Alcira María del Carmen cyanide cytochrome c oxidase porphobilinogen synthase s adenosylmethionine thiosulfate thiosulfate sulfurtransferase animal tissue article controlled study enzyme activity liver homogenate mouse nonhuman priority journal Animal Cyanides Cytochrome-c Oxidase In Vitro Liver Mice Porphobilinogen Synthase S-Adenosylmethionine Support, Non-U.S. Gov't Thiosulfate Sulfurtransferase Thiosulfates 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. Fil:Buzaleh, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Vazquez, E.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Del Carmen Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1991 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03063623_v22_n2_p281_Buzaleh http://hdl.handle.net/20.500.12110/paper_03063623_v22_n2_p281_Buzaleh
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic cyanide
cytochrome c oxidase
porphobilinogen synthase
s adenosylmethionine
thiosulfate
thiosulfate sulfurtransferase
animal tissue
article
controlled study
enzyme activity
liver homogenate
mouse
nonhuman
priority journal
Animal
Cyanides
Cytochrome-c Oxidase
In Vitro
Liver
Mice
Porphobilinogen Synthase
S-Adenosylmethionine
Support, Non-U.S. Gov't
Thiosulfate Sulfurtransferase
Thiosulfates
spellingShingle cyanide
cytochrome c oxidase
porphobilinogen synthase
s adenosylmethionine
thiosulfate
thiosulfate sulfurtransferase
animal tissue
article
controlled study
enzyme activity
liver homogenate
mouse
nonhuman
priority journal
Animal
Cyanides
Cytochrome-c Oxidase
In Vitro
Liver
Mice
Porphobilinogen Synthase
S-Adenosylmethionine
Support, Non-U.S. Gov't
Thiosulfate Sulfurtransferase
Thiosulfates
Buzaleh, Ana María
Vázquez, Elba Susana
Batlle, Alcira María del Carmen
In vitro effect of cyanide, thiosulphate and S-adenosyl-l-methionine on the activity of rhodanese and other enzymes
topic_facet cyanide
cytochrome c oxidase
porphobilinogen synthase
s adenosylmethionine
thiosulfate
thiosulfate sulfurtransferase
animal tissue
article
controlled study
enzyme activity
liver homogenate
mouse
nonhuman
priority journal
Animal
Cyanides
Cytochrome-c Oxidase
In Vitro
Liver
Mice
Porphobilinogen Synthase
S-Adenosylmethionine
Support, Non-U.S. Gov't
Thiosulfate Sulfurtransferase
Thiosulfates
description 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.
author Buzaleh, Ana María
Vázquez, Elba Susana
Batlle, Alcira María del Carmen
author_facet Buzaleh, Ana María
Vázquez, Elba Susana
Batlle, Alcira María del Carmen
author_sort Buzaleh, Ana María
title In vitro effect of cyanide, thiosulphate and S-adenosyl-l-methionine on the activity of rhodanese and other enzymes
title_short In vitro effect of cyanide, thiosulphate and S-adenosyl-l-methionine on the activity of rhodanese and other enzymes
title_full In vitro effect of cyanide, thiosulphate and S-adenosyl-l-methionine on the activity of rhodanese and other enzymes
title_fullStr In vitro effect of cyanide, thiosulphate and S-adenosyl-l-methionine on the activity of rhodanese and other enzymes
title_full_unstemmed In vitro effect of cyanide, thiosulphate and S-adenosyl-l-methionine on the activity of rhodanese and other enzymes
title_sort in vitro effect of cyanide, thiosulphate and s-adenosyl-l-methionine on the activity of rhodanese and other enzymes
publishDate 1991
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03063623_v22_n2_p281_Buzaleh
http://hdl.handle.net/20.500.12110/paper_03063623_v22_n2_p281_Buzaleh
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