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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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

id	paper:paper_10399712_v47_n2_p283_FlorinChristensen
record_format	dspace
spelling	paper:paper_10399712_v47_n2_p283_FlorinChristensen2023-06-08T16:00:36Z Lysosomal glycerophosphocholine phosphodiesterase in Tetrahymena 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 Tetrahymena Eukaryota Protozoa Tetrahymena Tetrahymena thermophila 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, it is sedimentable, shows a latency similar to that of acid phosphatase and is co-secreted with this enzyme, indicating that it is a lysosomal hydrolase. PNPPC-PDE was purified to homogeneity from the extracellular medium, yielding a single band of 58 kD on SDS polyacrylamide gel electrophoresis. It catalyzed the release of glycerol from glycerophosphocholine (GPC) and GPC competitively inhibits degradation of PNPPC. We present further evidence indicating that the natural substrate for PNPPC-PDE is GPC. Thus, Tetrahymena becomes the first eukaryote in which a lysosomal GPC-PDE is observed. This finding provides a new pathway for the complete breakdown of phosphatidylcholine in a lysosomal medium. 1999 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
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	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 Tetrahymena Eukaryota Protozoa Tetrahymena Tetrahymena thermophila
spellingShingle	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 Tetrahymena Eukaryota Protozoa Tetrahymena Tetrahymena thermophila Lysosomal glycerophosphocholine phosphodiesterase in Tetrahymena
topic_facet	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 Tetrahymena Eukaryota Protozoa Tetrahymena Tetrahymena thermophila
description	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, it is sedimentable, shows a latency similar to that of acid phosphatase and is co-secreted with this enzyme, indicating that it is a lysosomal hydrolase. PNPPC-PDE was purified to homogeneity from the extracellular medium, yielding a single band of 58 kD on SDS polyacrylamide gel electrophoresis. It catalyzed the release of glycerol from glycerophosphocholine (GPC) and GPC competitively inhibits degradation of PNPPC. We present further evidence indicating that the natural substrate for PNPPC-PDE is GPC. Thus, Tetrahymena becomes the first eukaryote in which a lysosomal GPC-PDE is observed. This finding provides a new pathway for the complete breakdown of phosphatidylcholine in a lysosomal medium.
title	Lysosomal glycerophosphocholine phosphodiesterase in Tetrahymena
title_short	Lysosomal glycerophosphocholine phosphodiesterase in Tetrahymena
title_full	Lysosomal glycerophosphocholine phosphodiesterase in Tetrahymena
title_fullStr	Lysosomal glycerophosphocholine phosphodiesterase in Tetrahymena
title_full_unstemmed	Lysosomal glycerophosphocholine phosphodiesterase in Tetrahymena
title_sort	lysosomal glycerophosphocholine phosphodiesterase in tetrahymena
publishDate	1999
url	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
_version_	1768542748554559488

Lysosomal glycerophosphocholine phosphodiesterase in Tetrahymena

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