1. The effect of ouabain on the molecular properties of (Na+/K+)-ATPase has been studied in purified preparations of the enzyme, isolated from the microsomal fraction of outer red medulla of porcine kidney, according to a modification of the method described by Jorgensen. 2. Ouabain, a specific inhibitor of (Na+/K+)-ATPase, binds at the potassium site of the enzyme, thus generating an increase in its stability towards the common denaturing agents, such as exposure to different concentration of guanidinium chloride (GdmC1) or to acidic solutions.

[Fluorescent properties of (Na+/K+)ATPase] / S., Grimaldi; D., Pozzi; Pascale, Esterina; M., D'Onofrio; Verna, Roberto; G., Giganti; F., Monaco; J., Roche. - In: COMPTES RENDUS DES SEANCES DE LA SOCIETE DE BIOLOGIE ET DE SES FILIALES. - ISSN 0037-9026. - 181:6(1987).

[Fluorescent properties of (Na+/K+)ATPase].

PASCALE, ESTERINA;VERNA, Roberto;
1987

Abstract

1. The effect of ouabain on the molecular properties of (Na+/K+)-ATPase has been studied in purified preparations of the enzyme, isolated from the microsomal fraction of outer red medulla of porcine kidney, according to a modification of the method described by Jorgensen. 2. Ouabain, a specific inhibitor of (Na+/K+)-ATPase, binds at the potassium site of the enzyme, thus generating an increase in its stability towards the common denaturing agents, such as exposure to different concentration of guanidinium chloride (GdmC1) or to acidic solutions.
1987
01 Pubblicazione su rivista::01a Articolo in rivista
[Fluorescent properties of (Na+/K+)ATPase] / S., Grimaldi; D., Pozzi; Pascale, Esterina; M., D'Onofrio; Verna, Roberto; G., Giganti; F., Monaco; J., Roche. - In: COMPTES RENDUS DES SEANCES DE LA SOCIETE DE BIOLOGIE ET DE SES FILIALES. - ISSN 0037-9026. - 181:6(1987).
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/431611
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