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 c...
Main Authors: | , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Instituto Oswaldo Cruz, Ministério da Saúde
1992-01-01
|
Series: | Memórias do Instituto Oswaldo Cruz. |
Subjects: | |
Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761992000500045 |
id |
doaj-42f8370c6f454163b004c00643823c16 |
---|---|
record_format |
Article |
spelling |
doaj-42f8370c6f454163b004c00643823c162020-11-25T01:33:45ZengInstituto Oswaldo Cruz, Ministério da SaúdeMemórias do Instituto Oswaldo Cruz.0074-02761678-80601992-01-018724124610.1590/S0074-02761992000500045Superoxide dismutase from Trichuris ovis, inhibiton by benzimidazoles and pyrimidine derivativesM. Sanchez-MorenoL. Garcia-RejonI. SalasA. OsunaM. MonteolivaThree 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.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761992000500045Trichuris ovissuperoxide dismutasecharacterizationinhibition |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
M. Sanchez-Moreno L. Garcia-Rejon I. Salas A. Osuna M. Monteoliva |
spellingShingle |
M. Sanchez-Moreno L. Garcia-Rejon I. Salas A. Osuna M. Monteoliva Superoxide dismutase from Trichuris ovis, inhibiton by benzimidazoles and pyrimidine derivatives Memórias do Instituto Oswaldo Cruz. Trichuris ovis superoxide dismutase characterization inhibition |
author_facet |
M. Sanchez-Moreno L. Garcia-Rejon I. Salas A. Osuna M. Monteoliva |
author_sort |
M. Sanchez-Moreno |
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 |
publisher |
Instituto Oswaldo Cruz, Ministério da Saúde |
series |
Memórias do Instituto Oswaldo Cruz. |
issn |
0074-0276 1678-8060 |
publishDate |
1992-01-01 |
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. |
topic |
Trichuris ovis superoxide dismutase characterization inhibition |
url |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761992000500045 |
work_keys_str_mv |
AT msanchezmoreno superoxidedismutasefromtrichurisovisinhibitonbybenzimidazolesandpyrimidinederivatives AT lgarciarejon superoxidedismutasefromtrichurisovisinhibitonbybenzimidazolesandpyrimidinederivatives AT isalas superoxidedismutasefromtrichurisovisinhibitonbybenzimidazolesandpyrimidinederivatives AT aosuna superoxidedismutasefromtrichurisovisinhibitonbybenzimidazolesandpyrimidinederivatives AT mmonteoliva superoxidedismutasefromtrichurisovisinhibitonbybenzimidazolesandpyrimidinederivatives |
_version_ |
1725075953661509632 |