Lysosomal glycerophosphocholine phosphodiesterase in Tetrahymena

The purification and characterization of a novel phosphodiesterase (PDE) is presented. The activity was detected in the extracellular medium of Tetrahymena thermophila cultures, by the release of p-nitrophenol from p-nitrophenylphosphocholine (PNPPC) with an acidic pH optimum. In cell homogenates, i...

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Detalles Bibliográficos
Publicado:	1999
Materias:	Extracellular hydrolase Glycerophosphocholine phosphodiesterase Lipid metabolism Lysosomal Tetrahymena 4 nitrophenol acid phosphatase choline (4 nitrophenyl phosphate) glycerol glycerophosphocholine phosphodiesterase glycerophosphorylcholine hydrolase phosphatidylcholine unclassified drug article cell free system culture medium degradation enzyme activity enzyme analysis enzyme purification enzyme substrate latent period lysosome nonhuman parasite cultivation pH polyacrylamide gel electrophoresis tetrahymena thermophila Animals Enzyme Stability Glycerylphosphorylcholine Hydrogen-Ion Concentration Kinetics Lysosomes Phosphatidylcholines Phosphoric Diester Hydrolases Phosphorylcholine Substrate Specificity Temperature Eukaryota Protozoa Tetrahymena thermophila
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10399712_v47_n2_p283_FlorinChristensen http://hdl.handle.net/20.500.12110/paper_10399712_v47_n2_p283_FlorinChristensen
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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