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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todo:paper_03063623_v22_n2_p281_Buzaleh2023-10-03T15:22:12Z In vitro effect of cyanide, thiosulphate and S-adenosyl-l-methionine on the activity of rhodanese and other enzymes Buzaleh, A.M. Vazquez, E.S. Del Carmen Batlle, A.M. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, A.M. Vazquez, E.S. Del Carmen Batlle, A.M. 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. |
format |
JOUR |
author |
Buzaleh, A.M. Vazquez, E.S. Del Carmen Batlle, A.M. |
author_facet |
Buzaleh, A.M. Vazquez, E.S. Del Carmen Batlle, A.M. |
author_sort |
Buzaleh, A.M. |
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 |
url |
http://hdl.handle.net/20.500.12110/paper_03063623_v22_n2_p281_Buzaleh |
work_keys_str_mv |
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_version_ |
1807320325554176000 |