Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity

Autores
Pinoni, Silvina Andrea; Goldemberg, Adriana Lia; Lopez Mañanes, Alejandra Antonia
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The occurrence, characteristics and response to environmental salinity of alkaline phosphatase (AP) activity were studied in chela muscle of the euryhaline crab Chasmagnathus granulatus from Mar Chiquita coastal lagoon (Buenos Aires Province, Argentina). Chela muscle exhibited a levamisole-insensitive and a levamisole-sensitive AP activities with distinct characteristics. Levamisole-insensitive activity appeared to be maximal at pH 7.7, whereas levamisole-sensitive AP activity was similar with the range of pH 7.4 to 8.0. Both activities at pH 7.7 exhibited a Michaelis-Menten kinetics (Km = 0.789 and 1.416 mM, respectively). I50 for levamisole-sensitive AP activity was about 12 mM. Levamisole-insensitive and levamisole-sensitive AP activities were differentially affected by temperature. Levamisole-sensitive AP activity was quite sensitive to temperature, exhibiting a peak at 37°C but being low at 5 to 30°C and 45 to 60°C. Both activities were inhibited by Cu2+. At 1.0 mM Cu2+, levamisole-insensitive AP activity was inhibited about 82% whereas levamisole-sensitive AP activity was almost completely inhibited. Levamisole-insensitive AP activity appeared to be sensitive to environmental salinity. In crabs acclimated to low salinity (10‰) this activity was lower than in 35‰ salinity. The response to environmental salinity suggests that levamisole-insensitive AP activity could be a component of muscle regulatory mechanisms at the biochemical level secondary to hyperregulation of C. granulatus. The possible physiological roles and functional relationship of AP activity with Na+/K+ ATPase in muscle are discussed.
Fil: Pinoni, Silvina Andrea. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Biología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina
Fil: Goldemberg, Adriana Lia. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Biología; Argentina
Fil: Lopez Mañanes, Alejandra Antonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Biología; Argentina
Materia
ALKALINE PHOSPHATASE
CHASMAGNATHUS GRANULATUS
CRABS
LEVAMISOLE
MUSCLE ENZYMES
OSMO-IONOREGULATION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/153151
Acceder
id CONICETDig_4710114fd5f3b431581da309c38cef7b
oai_identifier_str oai:ri.conicet.gov.ar:11336/153151
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinityPinoni, Silvina AndreaGoldemberg, Adriana LiaLopez Mañanes, Alejandra AntoniaALKALINE PHOSPHATASECHASMAGNATHUS GRANULATUSCRABSLEVAMISOLEMUSCLE ENZYMESOSMO-IONOREGULATIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The occurrence, characteristics and response to environmental salinity of alkaline phosphatase (AP) activity were studied in chela muscle of the euryhaline crab Chasmagnathus granulatus from Mar Chiquita coastal lagoon (Buenos Aires Province, Argentina). Chela muscle exhibited a levamisole-insensitive and a levamisole-sensitive AP activities with distinct characteristics. Levamisole-insensitive activity appeared to be maximal at pH 7.7, whereas levamisole-sensitive AP activity was similar with the range of pH 7.4 to 8.0. Both activities at pH 7.7 exhibited a Michaelis-Menten kinetics (Km = 0.789 and 1.416 mM, respectively). I50 for levamisole-sensitive AP activity was about 12 mM. Levamisole-insensitive and levamisole-sensitive AP activities were differentially affected by temperature. Levamisole-sensitive AP activity was quite sensitive to temperature, exhibiting a peak at 37°C but being low at 5 to 30°C and 45 to 60°C. Both activities were inhibited by Cu2+. At 1.0 mM Cu2+, levamisole-insensitive AP activity was inhibited about 82% whereas levamisole-sensitive AP activity was almost completely inhibited. Levamisole-insensitive AP activity appeared to be sensitive to environmental salinity. In crabs acclimated to low salinity (10‰) this activity was lower than in 35‰ salinity. The response to environmental salinity suggests that levamisole-insensitive AP activity could be a component of muscle regulatory mechanisms at the biochemical level secondary to hyperregulation of C. granulatus. The possible physiological roles and functional relationship of AP activity with Na+/K+ ATPase in muscle are discussed.Fil: Pinoni, Silvina Andrea. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Biología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; ArgentinaFil: Goldemberg, Adriana Lia. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Biología; ArgentinaFil: Lopez Mañanes, Alejandra Antonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Biología; ArgentinaElsevier Science2005-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/153151Pinoni, Silvina Andrea; Goldemberg, Adriana Lia; Lopez Mañanes, Alejandra Antonia; Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity; Elsevier Science; Journal of Experimental Marine Biology and Ecology; 326; 2; 12-2005; 217-2260022-0981CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0022098105002868info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jembe.2005.06.004info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:44:07Zoai:ri.conicet.gov.ar:11336/153151instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:44:07.941CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity
title Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity
spellingShingle Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity
Pinoni, Silvina Andrea
ALKALINE PHOSPHATASE
CHASMAGNATHUS GRANULATUS
CRABS
LEVAMISOLE
MUSCLE ENZYMES
OSMO-IONOREGULATION
title_short Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity
title_full Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity
title_fullStr Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity
title_full_unstemmed Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity
title_sort Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity
dc.creator.none.fl_str_mv Pinoni, Silvina Andrea
Goldemberg, Adriana Lia
Lopez Mañanes, Alejandra Antonia
author Pinoni, Silvina Andrea
author_facet Pinoni, Silvina Andrea
Goldemberg, Adriana Lia
Lopez Mañanes, Alejandra Antonia
author_role author
author2 Goldemberg, Adriana Lia
Lopez Mañanes, Alejandra Antonia
author2_role author
author
dc.subject.none.fl_str_mv ALKALINE PHOSPHATASE
CHASMAGNATHUS GRANULATUS
CRABS
LEVAMISOLE
MUSCLE ENZYMES
OSMO-IONOREGULATION
topic ALKALINE PHOSPHATASE
CHASMAGNATHUS GRANULATUS
CRABS
LEVAMISOLE
MUSCLE ENZYMES
OSMO-IONOREGULATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The occurrence, characteristics and response to environmental salinity of alkaline phosphatase (AP) activity were studied in chela muscle of the euryhaline crab Chasmagnathus granulatus from Mar Chiquita coastal lagoon (Buenos Aires Province, Argentina). Chela muscle exhibited a levamisole-insensitive and a levamisole-sensitive AP activities with distinct characteristics. Levamisole-insensitive activity appeared to be maximal at pH 7.7, whereas levamisole-sensitive AP activity was similar with the range of pH 7.4 to 8.0. Both activities at pH 7.7 exhibited a Michaelis-Menten kinetics (Km = 0.789 and 1.416 mM, respectively). I50 for levamisole-sensitive AP activity was about 12 mM. Levamisole-insensitive and levamisole-sensitive AP activities were differentially affected by temperature. Levamisole-sensitive AP activity was quite sensitive to temperature, exhibiting a peak at 37°C but being low at 5 to 30°C and 45 to 60°C. Both activities were inhibited by Cu2+. At 1.0 mM Cu2+, levamisole-insensitive AP activity was inhibited about 82% whereas levamisole-sensitive AP activity was almost completely inhibited. Levamisole-insensitive AP activity appeared to be sensitive to environmental salinity. In crabs acclimated to low salinity (10‰) this activity was lower than in 35‰ salinity. The response to environmental salinity suggests that levamisole-insensitive AP activity could be a component of muscle regulatory mechanisms at the biochemical level secondary to hyperregulation of C. granulatus. The possible physiological roles and functional relationship of AP activity with Na+/K+ ATPase in muscle are discussed.
Fil: Pinoni, Silvina Andrea. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Biología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina
Fil: Goldemberg, Adriana Lia. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Biología; Argentina
Fil: Lopez Mañanes, Alejandra Antonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Departamento de Biología; Argentina
description The occurrence, characteristics and response to environmental salinity of alkaline phosphatase (AP) activity were studied in chela muscle of the euryhaline crab Chasmagnathus granulatus from Mar Chiquita coastal lagoon (Buenos Aires Province, Argentina). Chela muscle exhibited a levamisole-insensitive and a levamisole-sensitive AP activities with distinct characteristics. Levamisole-insensitive activity appeared to be maximal at pH 7.7, whereas levamisole-sensitive AP activity was similar with the range of pH 7.4 to 8.0. Both activities at pH 7.7 exhibited a Michaelis-Menten kinetics (Km = 0.789 and 1.416 mM, respectively). I50 for levamisole-sensitive AP activity was about 12 mM. Levamisole-insensitive and levamisole-sensitive AP activities were differentially affected by temperature. Levamisole-sensitive AP activity was quite sensitive to temperature, exhibiting a peak at 37°C but being low at 5 to 30°C and 45 to 60°C. Both activities were inhibited by Cu2+. At 1.0 mM Cu2+, levamisole-insensitive AP activity was inhibited about 82% whereas levamisole-sensitive AP activity was almost completely inhibited. Levamisole-insensitive AP activity appeared to be sensitive to environmental salinity. In crabs acclimated to low salinity (10‰) this activity was lower than in 35‰ salinity. The response to environmental salinity suggests that levamisole-insensitive AP activity could be a component of muscle regulatory mechanisms at the biochemical level secondary to hyperregulation of C. granulatus. The possible physiological roles and functional relationship of AP activity with Na+/K+ ATPase in muscle are discussed.
publishDate 2005
dc.date.none.fl_str_mv 2005-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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://hdl.handle.net/11336/153151
Pinoni, Silvina Andrea; Goldemberg, Adriana Lia; Lopez Mañanes, Alejandra Antonia; Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity; Elsevier Science; Journal of Experimental Marine Biology and Ecology; 326; 2; 12-2005; 217-226
0022-0981
CONICET Digital
CONICET
url http://hdl.handle.net/11336/153151
identifier_str_mv Pinoni, Silvina Andrea; Goldemberg, Adriana Lia; Lopez Mañanes, Alejandra Antonia; Alkaline phosphatase activities in muscle of the euryhaline crab Chasmagnathus granulatus: Response to environmental salinity; Elsevier Science; Journal of Experimental Marine Biology and Ecology; 326; 2; 12-2005; 217-226
0022-0981
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0022098105002868
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jembe.2005.06.004
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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