Effect of vanadium compounds on acid phosphatase activity
- Autores
- Vescina, Cecilia M.; Sálice, Viviana C.; Cortizo, Ana María; Etcheverry, Susana B.
- Año de publicación
- 1996
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The direct effect of different vanadium compounds on acid phosphatase (ACP) activity was investigated. Vanadate and vanadyl but not pervanadate inhibited the wheat germ ACP activity. These vanadium derivatives did not alter the fibroblast Swiss 3T3 soluble fraction ACP activity. Using inhibitors of tyrosine phosphatases (PTPases), the wheat germ ACP was partially characterized as a PTPase. This study suggests that the inhibitory ability of different vanadium derivatives to modulate ACP activity seems to depend on the geometry around the vanadium atom more than on the oxidation state. Our results indicate a correlation between the PTPase activity and the sensitivity to vanadate and vanadyl cation.
Facultad de Ciencias Exactas - Materia
-
Ciencias Exactas
Química
Vanadio
vanadium, acid phosphatase, tyrosine-phosphatase, fibroblast cells, inhibitory effects - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/76255
Ver los metadatos del registro completo
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Effect of vanadium compounds on acid phosphatase activityVescina, Cecilia M.Sálice, Viviana C.Cortizo, Ana MaríaEtcheverry, Susana B.Ciencias ExactasQuímicaVanadiovanadium, acid phosphatase, tyrosine-phosphatase, fibroblast cells, inhibitory effectsThe direct effect of different vanadium compounds on acid phosphatase (ACP) activity was investigated. Vanadate and vanadyl but not pervanadate inhibited the wheat germ ACP activity. These vanadium derivatives did not alter the fibroblast Swiss 3T3 soluble fraction ACP activity. Using inhibitors of tyrosine phosphatases (PTPases), the wheat germ ACP was partially characterized as a PTPase. This study suggests that the inhibitory ability of different vanadium derivatives to modulate ACP activity seems to depend on the geometry around the vanadium atom more than on the oxidation state. Our results indicate a correlation between the PTPase activity and the sensitivity to vanadate and vanadyl cation.Facultad de Ciencias Exactas1996info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf185-191http://sedici.unlp.edu.ar/handle/10915/76255enginfo:eu-repo/semantics/altIdentifier/issn/0163-4984info:eu-repo/semantics/altIdentifier/hdl/11746/4413info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:13:25Zoai:sedici.unlp.edu.ar:10915/76255Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:13:25.78SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Effect of vanadium compounds on acid phosphatase activity |
title |
Effect of vanadium compounds on acid phosphatase activity |
spellingShingle |
Effect of vanadium compounds on acid phosphatase activity Vescina, Cecilia M. Ciencias Exactas Química Vanadio vanadium, acid phosphatase, tyrosine-phosphatase, fibroblast cells, inhibitory effects |
title_short |
Effect of vanadium compounds on acid phosphatase activity |
title_full |
Effect of vanadium compounds on acid phosphatase activity |
title_fullStr |
Effect of vanadium compounds on acid phosphatase activity |
title_full_unstemmed |
Effect of vanadium compounds on acid phosphatase activity |
title_sort |
Effect of vanadium compounds on acid phosphatase activity |
dc.creator.none.fl_str_mv |
Vescina, Cecilia M. Sálice, Viviana C. Cortizo, Ana María Etcheverry, Susana B. |
author |
Vescina, Cecilia M. |
author_facet |
Vescina, Cecilia M. Sálice, Viviana C. Cortizo, Ana María Etcheverry, Susana B. |
author_role |
author |
author2 |
Sálice, Viviana C. Cortizo, Ana María Etcheverry, Susana B. |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
Ciencias Exactas Química Vanadio vanadium, acid phosphatase, tyrosine-phosphatase, fibroblast cells, inhibitory effects |
topic |
Ciencias Exactas Química Vanadio vanadium, acid phosphatase, tyrosine-phosphatase, fibroblast cells, inhibitory effects |
dc.description.none.fl_txt_mv |
The direct effect of different vanadium compounds on acid phosphatase (ACP) activity was investigated. Vanadate and vanadyl but not pervanadate inhibited the wheat germ ACP activity. These vanadium derivatives did not alter the fibroblast Swiss 3T3 soluble fraction ACP activity. Using inhibitors of tyrosine phosphatases (PTPases), the wheat germ ACP was partially characterized as a PTPase. This study suggests that the inhibitory ability of different vanadium derivatives to modulate ACP activity seems to depend on the geometry around the vanadium atom more than on the oxidation state. Our results indicate a correlation between the PTPase activity and the sensitivity to vanadate and vanadyl cation. Facultad de Ciencias Exactas |
description |
The direct effect of different vanadium compounds on acid phosphatase (ACP) activity was investigated. Vanadate and vanadyl but not pervanadate inhibited the wheat germ ACP activity. These vanadium derivatives did not alter the fibroblast Swiss 3T3 soluble fraction ACP activity. Using inhibitors of tyrosine phosphatases (PTPases), the wheat germ ACP was partially characterized as a PTPase. This study suggests that the inhibitory ability of different vanadium derivatives to modulate ACP activity seems to depend on the geometry around the vanadium atom more than on the oxidation state. Our results indicate a correlation between the PTPase activity and the sensitivity to vanadate and vanadyl cation. |
publishDate |
1996 |
dc.date.none.fl_str_mv |
1996 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://sedici.unlp.edu.ar/handle/10915/76255 |
url |
http://sedici.unlp.edu.ar/handle/10915/76255 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/issn/0163-4984 info:eu-repo/semantics/altIdentifier/hdl/11746/4413 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
dc.format.none.fl_str_mv |
application/pdf 185-191 |
dc.source.none.fl_str_mv |
reponame:SEDICI (UNLP) instname:Universidad Nacional de La Plata instacron:UNLP |
reponame_str |
SEDICI (UNLP) |
collection |
SEDICI (UNLP) |
instname_str |
Universidad Nacional de La Plata |
instacron_str |
UNLP |
institution |
UNLP |
repository.name.fl_str_mv |
SEDICI (UNLP) - Universidad Nacional de La Plata |
repository.mail.fl_str_mv |
alira@sedici.unlp.edu.ar |
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1844616005007966208 |
score |
13.070432 |