Publication: Solubilización y caracterización de la actividad trehalasa ligada a la pared celular de ascosporas de schizzosaccharomyces pombe
Authors
Gacto Fernández, Mariano José ; Vicente Soler, Jerónima
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Facultad de Biología
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Publisher
Murcia: Universidad de Murcia, Servicio de Publicaciones
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Se ha investigado la localización de la trehalasa en ascosporas aisladas de Schiiosacchar~omycfs pombe
mediante un método citoquímico basado en la formación de complejos insolubles de eugenol, producidos
extracelularmente en una reacción acoplada a la actividad trehalasa. La mayor parte de la actividad enzimática
detectable en extractos celulares está unida a la pared celular de las ascosporas. Por tratamiento controlado de
paredes celulares con el sistema Iítico iiovoenzima es posible lograr una solubilización parcial de la trehalasa
particulada. El perfil de elución obtenido por filtración molecular del enzima solubilizado de paredes indica
una amplia heterogeneidad molecular, lo que sugiere una posible naturaleza glicoproteica del enzima. Los
ensayos de activación y el análisis de propiedades cinéticas revelan que esta actividad se debe a una trehalasa
de las pertenecientes al tipo no regulador
The location of trehalase in isolated ascospores from Schizosacchar-omyces pombe has been investigated by a cytochemical method based on the formation by eugenol of insoluble complexes that are produced extracellularly during a reaction coupled to the trehalase activity. Most of the enzyme activity present in cell extracts is linked to the ascospore cell wall. A partial solubilization of the particulate trehalase was achieved by controlled treatment of isolated cell walls with the lytic system novozym. The elution pattern obtaiiled by molecular filtration of the enzyme solubilized from the walls shows a broad molecular heterogeneity suggesting a possible glycoprotein nature of the enzyme. Assays for activation and analysis of kinetic properties revealed that this activity is due to a trehalase of the so-called nonregulatory type
The location of trehalase in isolated ascospores from Schizosacchar-omyces pombe has been investigated by a cytochemical method based on the formation by eugenol of insoluble complexes that are produced extracellularly during a reaction coupled to the trehalase activity. Most of the enzyme activity present in cell extracts is linked to the ascospore cell wall. A partial solubilization of the particulate trehalase was achieved by controlled treatment of isolated cell walls with the lytic system novozym. The elution pattern obtaiiled by molecular filtration of the enzyme solubilized from the walls shows a broad molecular heterogeneity suggesting a possible glycoprotein nature of the enzyme. Assays for activation and analysis of kinetic properties revealed that this activity is due to a trehalase of the so-called nonregulatory type
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