Artículo

Florin-Christensen, J.; Florin-Christensen, M. "Lysosomal glycerophosphocholine phosphodiesterase in Tetrahymena" (1999) Biochemistry and Molecular Biology International. 47(2):283-292
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Abstract:

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.

Registro:

Documento: Artículo
Título:Lysosomal glycerophosphocholine phosphodiesterase in Tetrahymena
Autor:Florin-Christensen, J.; Florin-Christensen, M.
Filiación:Institute of Neuroscience (INEUCI), Ciudad Universitaria, Pab. II, 4 Piso, (1428) Buenos Aries, Argentina
Palabras clave: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
Año:1999
Volumen:47
Número:2
Página de inicio:283
Página de fin:292
Título revista:Biochemistry and Molecular Biology International
Título revista abreviado:Biochem. Mol. Biol. Int.
ISSN:10399712
CODEN:BMBIE
CAS:4-nitrophenylphosphorylcholine; glycerophosphocholine phosphodiesterase, EC 3.1.4.2; Glycerylphosphorylcholine, 563-24-6; Phosphatidylcholines; Phosphoric Diester Hydrolases, EC 3.1.4.-; Phosphorylcholine, 107-73-3
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10399712_v47_n2_p283_FlorinChristensen

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Citas:

---------- APA ----------
Florin-Christensen, J. & Florin-Christensen, M. (1999) . Lysosomal glycerophosphocholine phosphodiesterase in Tetrahymena. Biochemistry and Molecular Biology International, 47(2), 283-292.
Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10399712_v47_n2_p283_FlorinChristensen [ ]
---------- CHICAGO ----------
Florin-Christensen, J., Florin-Christensen, M. "Lysosomal glycerophosphocholine phosphodiesterase in Tetrahymena" . Biochemistry and Molecular Biology International 47, no. 2 (1999) : 283-292.
Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10399712_v47_n2_p283_FlorinChristensen [ ]
---------- MLA ----------
Florin-Christensen, J., Florin-Christensen, M. "Lysosomal glycerophosphocholine phosphodiesterase in Tetrahymena" . Biochemistry and Molecular Biology International, vol. 47, no. 2, 1999, pp. 283-292.
Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10399712_v47_n2_p283_FlorinChristensen [ ]
---------- VANCOUVER ----------
Florin-Christensen, J., Florin-Christensen, M. Lysosomal glycerophosphocholine phosphodiesterase in Tetrahymena. Biochem. Mol. Biol. Int. 1999;47(2):283-292.
Available from: https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10399712_v47_n2_p283_FlorinChristensen [ ]