Estimation of a Few Nanograms of Fluoride in Presence of Phosphate by Use of Liver Esterase.

McGaughey, C.A.; Stowell, Ellery C.

doi:10.1021/ac60218a037

Cited by 19 publications

(5 citation statements)

References 15 publications

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“…Two reported inhibitors of phosphatidate phosphohydrolase, sodium fluoride (Caras and Shapiro 1975) and propranolol (Koul and Hauser 1987), were used to selectively block the phosphatase. Sodium fluoride, an inhibitor of a wide variety of metal ion dependent and independent enzymes (McGaughey and Stowell 1964;Sedgwick and Hubscher 1967;Bunick and Kashket 1982), inhibited [14c]diglyceride generation in a dosedependent manner. However, concentrations 1 4 0 pM inhibited the PLD-mediated release of phosphatidic acid.…”

Section: Discussionmentioning

confidence: 99%

Use of [1-¹⁴C]oleate labelled autoclaved Escherichia coli as a membranous substrate for measurement of in vitro phospholipase D activity

Ghosh¹,

Franson²

1992

Biochem. Cell Biol.

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Autoclaved Escherichia coli labelled with [1-14C]oleate in the 2-acyl position have been used extensively to measure phospholipase A2 activity in vitro. The present study demonstrates that this membranous substrate is also useful for the measurement of in vitro phospholipase D activity. Phospholipase D from Streptomyces chromofuscus catalyzed the hydrolysis of [1-14C]oleate labelled, autoclaved E. coli optimally at pH 7.0-8.0 to generate [14C]phosphatidic acid in the presence of 5 mM added Ca2+. Other divalent cations would not substitute for Ca2+. Activity was linear with time and protein up to 30% of the hydrolysis of substrate. Phospholipase D activity was stimulated in a dose-dependent manner by the addition of Triton X-100. The activity was increased 5.5-fold with 0.05% Triton, a concentration that totally inhibited hydrolysis of E. coli by human synovial fluid phospholipase A2. Accumulation of [14C]diglyceride was observed after 10 min of incubation. This accumulation was inhibited by NaF (IC50 = 18 microM) or propanolol (IC50 = 180 microM) suggesting the S. chromofuscus phospholipase D was contaminated with phosphatidate phosphohydrolase. Phosphatidic acid released by the action of cabbage phospholipase D was converted to phosphatidylethanol in an ethanol concentration dependent manner. These results demonstrate that [1-14C]oleate labelled, autoclaved E. coli can be used to measure phospholipase D activity by monitoring accumulation of either [14C]phosphatidic acid or [14C]phosphatidylethanol.

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Section: Discussionmentioning

confidence: 99%

Use of [1-¹⁴C]oleate labelled autoclaved Escherichia coli as a membranous substrate for measurement of in vitro phospholipase D activity

Ghosh¹,

Franson²

1992

Biochem. Cell Biol.

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“…A simultaneous method for the determination of zirconium and hafnium has been proposed (170); a kinetic method for the microdetermination of osmium has been described (169); and an ultramicromethod to determine cobalt in phosphorus has been developed (116). Catalytic effects have been employed in the amperometric determination of microgram amounts of germanium (99); a catalytic fluorescence reaction has been proposed for the determination of copper (80); and fluorides have been determined in the nanogram range by a method involving the use of liver esterase (90), in which enzyme activity was measured by the titration of butyric acid formed from ethyl butyrate with sodium hydroxide.…”

Section: Catalytic Methodsmentioning

confidence: 99%

Inorganic Microchemistry

West¹

1966

Anal. Chem.

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The be view of inorganic microchemistry is contiguous with the previous review (160) and extends through December 1965. Because many techniques such as chromatography, ion exchange, extraction, nucleonics, spectroscopy, and microscopy, which are of importance in inorganic microchemistry, are reviewed as separate topics, only brief mention will be made of them in this discussion and the reader is referred to the accompanying specialized reviews for more complete orientation.It is obvious from the previous reviews of inorganic microchemistry that no real distinction is made between trace analysis and microchemistry, although many specialists feel that there is a great difference between these fields. This reviewer feels that the problems of trace studies and microanalysis are often so

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“…Linde (134). The liver esterase that is specifically inhibited by fluoride was assayed either by a pH titration of the butyric acid formed in the enzymic hydrolysis of ethyl butyrate (143) or colorimetrically (134). Shaw (222) has reported that Cu+2, Zn+2 and Ni+2 in 10_7to 10_6Jf concentrations, and Co+2, Fe+2, and Mn+2 in 5 X 10~5 to 10-W concentrations inhibit urease and may be determined.…”

Section: Billiar Andmentioning

confidence: 99%

“…Other muco-polysaccharides do not interfere. A specific method for the determination of nanogram quantities of fluoride in the presence of phosphate was described by McGaughey and Stowell(143) and…”

mentioning

confidence: 99%

Use of Enzymes in Analytical Chemistry

Guilbault¹

1966

Anal. Chem.

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Estimation of a Few Nanograms of Fluoride in Presence of Phosphate by Use of Liver Esterase.

Cited by 19 publications

References 15 publications

Use of [1-¹⁴C]oleate labelled autoclaved Escherichia coli as a membranous substrate for measurement of in vitro phospholipase D activity

Use of [1-¹⁴C]oleate labelled autoclaved Escherichia coli as a membranous substrate for measurement of in vitro phospholipase D activity

Inorganic Microchemistry

Use of Enzymes in Analytical Chemistry

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Estimation of a Few Nanograms of Fluoride in Presence of Phosphate by Use of Liver Esterase.

Cited by 19 publications

References 15 publications

Use of [1-14C]oleate labelled autoclaved Escherichia coli as a membranous substrate for measurement of in vitro phospholipase D activity

Use of [1-14C]oleate labelled autoclaved Escherichia coli as a membranous substrate for measurement of in vitro phospholipase D activity

Inorganic Microchemistry

Use of Enzymes in Analytical Chemistry

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Product

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Use of [1-¹⁴C]oleate labelled autoclaved Escherichia coli as a membranous substrate for measurement of in vitro phospholipase D activity

Use of [1-¹⁴C]oleate labelled autoclaved Escherichia coli as a membranous substrate for measurement of in vitro phospholipase D activity