Hydrolysis of triphosphoinositides by a soluble fraction of Crithidia fasciculata

F. B.St C. Palmer

doi:10.1016/0005-2760(76)90244-7

Hydrolysis of triphosphoinositides by a soluble fraction of Crithidia fasciculata

F. B.St C. Palmer

Medicine

Medicine

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9 Citations (Scopus)

Abstract

Homogenates of Crithidia fasciculata (a species of Trypanosomidae) were shown to contain a phosphatase (EC 3.1.3.36) and a phosphodiesterase (EC 3.1.4.11) which hydrolyse triphosphoinositides. Approximately 30% of the diesterase and most of the phosphatase are present in the soluble fraction. The triphosphoinositide phosphatase is specifically dependent upon Mg²⁺ and is stable to storage with or without freezing. The triphosphoinositide phosphodiesterase requires Ca²⁺ and is inactivated during storage. Both activities are maximal in the presence of cetyltrimethylammonium bromide and require protection or reactivation by GSH or dithiothreitol. Unlike similar mammalian enzymes the protozoal triphosphoinositide phosphatase does not hydrolyse diphosphoinositides. The two enzymes may be separated by (NH₄)₂SO₄ fractionation and gel filtration on Sephadex G-200.

Original language	English
Pages (from-to)	477-487
Number of pages	11
Journal	Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Volume	441
Issue number	3
DOIs	https://doi.org/10.1016/0005-2760(76)90244-7
Publication status	Published - Sept 27 1976

Bibliographical note

Funding Information:
This work was supported by the Medical Research Council of Canada. The technical assistanceo f Miss Michelle Roberge and Mrs. Gladys Keddy was greatly appreciated.

ASJC Scopus Subject Areas

Biophysics
Biochemistry
Endocrinology

PubMed: MeSH publication types

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title = "Hydrolysis of triphosphoinositides by a soluble fraction of Crithidia fasciculata",

abstract = "Homogenates of Crithidia fasciculata (a species of Trypanosomidae) were shown to contain a phosphatase (EC 3.1.3.36) and a phosphodiesterase (EC 3.1.4.11) which hydrolyse triphosphoinositides. Approximately 30% of the diesterase and most of the phosphatase are present in the soluble fraction. The triphosphoinositide phosphatase is specifically dependent upon Mg2+ and is stable to storage with or without freezing. The triphosphoinositide phosphodiesterase requires Ca2+ and is inactivated during storage. Both activities are maximal in the presence of cetyltrimethylammonium bromide and require protection or reactivation by GSH or dithiothreitol. Unlike similar mammalian enzymes the protozoal triphosphoinositide phosphatase does not hydrolyse diphosphoinositides. The two enzymes may be separated by (NH4)2SO4 fractionation and gel filtration on Sephadex G-200.",

author = "Palmer, {F. B.St C.}",

note = "Funding Information: This work was supported by the Medical Research Council of Canada. The technical assistanceo f Miss Michelle Roberge and Mrs. Gladys Keddy was greatly appreciated.",

year = "1976",

month = sep,

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doi = "10.1016/0005-2760(76)90244-7",

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T1 - Hydrolysis of triphosphoinositides by a soluble fraction of Crithidia fasciculata

AU - Palmer, F. B.St C.

N1 - Funding Information: This work was supported by the Medical Research Council of Canada. The technical assistanceo f Miss Michelle Roberge and Mrs. Gladys Keddy was greatly appreciated.

PY - 1976/9/27

Y1 - 1976/9/27

N2 - Homogenates of Crithidia fasciculata (a species of Trypanosomidae) were shown to contain a phosphatase (EC 3.1.3.36) and a phosphodiesterase (EC 3.1.4.11) which hydrolyse triphosphoinositides. Approximately 30% of the diesterase and most of the phosphatase are present in the soluble fraction. The triphosphoinositide phosphatase is specifically dependent upon Mg2+ and is stable to storage with or without freezing. The triphosphoinositide phosphodiesterase requires Ca2+ and is inactivated during storage. Both activities are maximal in the presence of cetyltrimethylammonium bromide and require protection or reactivation by GSH or dithiothreitol. Unlike similar mammalian enzymes the protozoal triphosphoinositide phosphatase does not hydrolyse diphosphoinositides. The two enzymes may be separated by (NH4)2SO4 fractionation and gel filtration on Sephadex G-200.

AB - Homogenates of Crithidia fasciculata (a species of Trypanosomidae) were shown to contain a phosphatase (EC 3.1.3.36) and a phosphodiesterase (EC 3.1.4.11) which hydrolyse triphosphoinositides. Approximately 30% of the diesterase and most of the phosphatase are present in the soluble fraction. The triphosphoinositide phosphatase is specifically dependent upon Mg2+ and is stable to storage with or without freezing. The triphosphoinositide phosphodiesterase requires Ca2+ and is inactivated during storage. Both activities are maximal in the presence of cetyltrimethylammonium bromide and require protection or reactivation by GSH or dithiothreitol. Unlike similar mammalian enzymes the protozoal triphosphoinositide phosphatase does not hydrolyse diphosphoinositides. The two enzymes may be separated by (NH4)2SO4 fractionation and gel filtration on Sephadex G-200.

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JO - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

JF - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

IS - 3

ER -

Hydrolysis of triphosphoinositides by a soluble fraction of Crithidia fasciculata

Abstract

Bibliographical note

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PubMed: MeSH publication types

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