Superoxide dismutase from Trichuris ovis, inhibiton by benzimidazoles and pyrimidine derivatives

Three superoxide dismutase isoenzymes of different cellular location were detected in an homogenate of Thrichuris ovis. Each of these molecular forms was purified by differential centrifugation and precipitation with ammonium sulphate, followed by chromatography on DEAE-cellulose and Sephadex G-75 columns. The activity levels of the two molecular forms detected in the mitochondrial (one cyanide sensitive Cu-Zn-SOD and the other cyanide intensitive Mn-Sod were higher than that of the superoxide dismutase detected in the cytoplasmic fraction (cyanid sensitive Cu-Zn-SOD). All the mollecular forms present evident differences to the SODs contained in the host liver. Molecular mass and some of the physical and chemical aproperties of the enzyme was determined for all three molecular forms. An inhibitory effect on the SOD of the parasite an the host was detected with a series of compounds, some of wich markedly inhibited parasite ensyme but not host enzyme.

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Main Authors: Sanchez-Moreno,M., Garcia-Rejon,L., Salas,I., Osuna,A., Monteoliva,M.
Format: Digital revista
Language:English
Published: Instituto Oswaldo Cruz, Ministério da Saúde 1992
Online Access:http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761992000500045
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spelling oai:scielo:S0074-027619920005000452009-06-15Superoxide dismutase from Trichuris ovis, inhibiton by benzimidazoles and pyrimidine derivativesSanchez-Moreno,M.Garcia-Rejon,L.Salas,I.Osuna,A.Monteoliva,M. Trichuris ovis superoxide dismutase characterization inhibition Three superoxide dismutase isoenzymes of different cellular location were detected in an homogenate of Thrichuris ovis. Each of these molecular forms was purified by differential centrifugation and precipitation with ammonium sulphate, followed by chromatography on DEAE-cellulose and Sephadex G-75 columns. The activity levels of the two molecular forms detected in the mitochondrial (one cyanide sensitive Cu-Zn-SOD and the other cyanide intensitive Mn-Sod were higher than that of the superoxide dismutase detected in the cytoplasmic fraction (cyanid sensitive Cu-Zn-SOD). All the mollecular forms present evident differences to the SODs contained in the host liver. Molecular mass and some of the physical and chemical aproperties of the enzyme was determined for all three molecular forms. An inhibitory effect on the SOD of the parasite an the host was detected with a series of compounds, some of wich markedly inhibited parasite ensyme but not host enzyme.info:eu-repo/semantics/openAccessInstituto Oswaldo Cruz, Ministério da SaúdeMemórias do Instituto Oswaldo Cruz v.87 suppl.1 19921992-01-01info:eu-repo/semantics/articletext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761992000500045en10.1590/S0074-02761992000500045
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libraryname SciELO
language English
format Digital
author Sanchez-Moreno,M.
Garcia-Rejon,L.
Salas,I.
Osuna,A.
Monteoliva,M.
spellingShingle Sanchez-Moreno,M.
Garcia-Rejon,L.
Salas,I.
Osuna,A.
Monteoliva,M.
Superoxide dismutase from Trichuris ovis, inhibiton by benzimidazoles and pyrimidine derivatives
author_facet Sanchez-Moreno,M.
Garcia-Rejon,L.
Salas,I.
Osuna,A.
Monteoliva,M.
author_sort Sanchez-Moreno,M.
title Superoxide dismutase from Trichuris ovis, inhibiton by benzimidazoles and pyrimidine derivatives
title_short Superoxide dismutase from Trichuris ovis, inhibiton by benzimidazoles and pyrimidine derivatives
title_full Superoxide dismutase from Trichuris ovis, inhibiton by benzimidazoles and pyrimidine derivatives
title_fullStr Superoxide dismutase from Trichuris ovis, inhibiton by benzimidazoles and pyrimidine derivatives
title_full_unstemmed Superoxide dismutase from Trichuris ovis, inhibiton by benzimidazoles and pyrimidine derivatives
title_sort superoxide dismutase from trichuris ovis, inhibiton by benzimidazoles and pyrimidine derivatives
description Three superoxide dismutase isoenzymes of different cellular location were detected in an homogenate of Thrichuris ovis. Each of these molecular forms was purified by differential centrifugation and precipitation with ammonium sulphate, followed by chromatography on DEAE-cellulose and Sephadex G-75 columns. The activity levels of the two molecular forms detected in the mitochondrial (one cyanide sensitive Cu-Zn-SOD and the other cyanide intensitive Mn-Sod were higher than that of the superoxide dismutase detected in the cytoplasmic fraction (cyanid sensitive Cu-Zn-SOD). All the mollecular forms present evident differences to the SODs contained in the host liver. Molecular mass and some of the physical and chemical aproperties of the enzyme was determined for all three molecular forms. An inhibitory effect on the SOD of the parasite an the host was detected with a series of compounds, some of wich markedly inhibited parasite ensyme but not host enzyme.
publisher Instituto Oswaldo Cruz, Ministério da Saúde
publishDate 1992
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761992000500045
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