In situ measurement of cAMP related enzymes in the dimorphic fungus Mucor rouxii

Yeast cells of the dimorphic fungus Mucor rouxii have been permeabilized by treatment with toluene:ethanol. The permeabilization allowed the in situ measurement of pyruvate kinase, cAMP phosphodiesterase and adenylate cyclase activities. Using a small peptide as substrate, cAMP dependent protein kin...

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Detalles Bibliográficos
Autores principales: Maggese, M.C., Galvagno, M.A., Cantore, M.L., Passeron, S.
Formato: JOUR
Materias:
3',5' cyclic nucleotide phosphodiesterase
adenylate cyclase
cyclic AMP
protein kinase
pyruvate kinase
toluene
article
comparative study
metabolism
Mucor
permeability
3',5'-Cyclic-Nucleotide Phosphodiesterase
Adenylate Cyclase
Comparative Study
Cyclic AMP
Permeability
Protein Kinases
Pyruvate Kinase
Support, Non-U.S. Gov't
Toluene
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_03091651_v6_n12_p1101_Maggese
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario:Yeast cells of the dimorphic fungus Mucor rouxii have been permeabilized by treatment with toluene:ethanol. The permeabilization allowed the in situ measurement of pyruvate kinase, cAMP phosphodiesterase and adenylate cyclase activities. Using a small peptide as substrate, cAMP dependent protein kinase activity could also be measured. Permeabilized cells showed higher cAMP phosphodiesterase and adenylate cyclase activities than cellular homogenates. The main catalytic properties of the enzymes were similar to that previously found in in vitro studies. © 1982.

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