Cytochemical localization of acid phosphatase in Stigeoclonium tenue (Chaetophorales, Chlorophyceae)

Nonspecific acid phosphatases are a group of enzymes whose activity increases the availability of exogenous and endogenous orthophosphate either through extra- or intracellular hydrolysis of phosphate compounds. Our study demonstrates the activity of acid phosphatases in the filamentous freshwater a...

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Detalles Bibliográficos
Autores: Michetti, Karina Mariel, Leonardi, Patricia Ines, Caceres, Eduardo Jorge
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2006
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/34863
Acceso en línea:http://hdl.handle.net/11336/34863
Access Level:acceso abierto
Palabra clave:CHAETOPHORALES
ACID PHOSPHATASE
STIGEOCLONIUM TENUE
ULTRASTRUCTURE
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
Descripción
Sumario:Nonspecific acid phosphatases are a group of enzymes whose activity increases the availability of exogenous and endogenous orthophosphate either through extra- or intracellular hydrolysis of phosphate compounds. Our study demonstrates the activity of acid phosphatases in the filamentous freshwater alga Stigeoclonium tenue. These enzymes were detected following a cerium-based method in which cerium was used as an orthophosphate-capture reagent. In thalli from S. tenue from the natural environment, acid phosphatases were found in the longitudinal cell wall, plasmalemma, and vacuole. In thalli from Bold’s Basal Medium culture, these enzymes were found mainly in the plasmalemma; they were scarce in the cell wall. In the thalli grown in phosphate-enriched culture medium, enzymes were found only in the plasmalemma. The low availability of orthophosphate in the medium seems to induce the transport of these enzymes to the cell wall. Its abundance, on the contrary, seems to attenuate this response without affecting the localization of acid phosphatases in the plasmalemma.