Comparative effects, in vitro, of various detergents on liver glucose-6-phosphate phosphohydrolase, inorganic pyrophosphate-glucose phosphotransferase, and acid inorganic pyrophosphatase activities

Snoke, Roy E.; Nordlie, Robert C.

doi:10.1016/0005-2744(67)90131-3

Cited by 32 publications

(1 citation statement)

References 11 publications

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“…Glucose 6-phosphatase preparations are very sensitive to a variety of detergents used for purification. Some detergents activate at low concentration and inhibit at high concentrations, while others only inhibit (Beaufay and de Duve 1954a;Carruthers and Baumler, 1962;Snoke and Nordlie, 1967).…”

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Purification, characterization and initial rate kinetics of acyl-phosphate-hexose phosphotransferase from Aerobacter aerogenes

Casazza

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mentioning

confidence: 99%

Purification, characterization and initial rate kinetics of acyl-phosphate-hexose phosphotransferase from Aerobacter aerogenes

Casazza

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Glucose-6-phosphatase

Nordlie

Jorgenson

1976

The Enzymes of Bioligical Membranes

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A new, sensitive determination of phosphate

Eibl

Lands

1969

Analytical Biochemistry

486

118

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Many published methods for the spectrophotometric determination of phosphorus have been based on the original method of Bell and Doisy (1). These methods generally depend on developing a specific blue color of the phosphomolybdate complex in the presence of reducing agents such as hydroquinone (l-3)) 1,2,4-aminonaphtholsulfonic acid (P6), and ascorbic acid (7-9). Bartlett (6) improved the sensitivity of the widely used method of Fiske and SubbaRow (4). Heating at 100°C resulted in a 7.2-fold increase in sensitivity with a molar absorbance at 830 nm of 2.6 X lo4 M-%rn-l in comparison to 3.6 x 10" M-*cm-* at 660 nm obtained with the other procedures. Application of the method was limited however to the determination of total phosphorus as described by Bartlett (6) : "The phosphorus heating method could not be used to assay inorganic orthophosphate in the presence of a number of phosphate esters which hydrolyzed under these conditions. The original Fiske and SubbaRow method was found most reliable for measuring inorganic phosphate when mixed with phosphate esters." The enzymic activities of phosphatases, which release free phosphate from organic phosphate esters, are determined by measuring the liberated phosphate in the presence of the unreacted phosphate ester substrates. Phosphatases in tissue homogenates or preparations of subcellular particles may be made more accessible to substrate by adding solubilizing agents. However, application of the Fiske and SubbaRow method (4) to such enzymic assays often caused errors when Triton X-100 was used in the system. For instance Wattiaux and de Duve used 0.1% Triton X-100 in the incubation mixtures (10). They reported that "control experiments showed that the detergent was without inhibitory effect on any of the enzymes studied, but that it could interfere with the analytical procedures used in the phosphatase assays." In addition, Snoke and Nordlie (11) commented that "deoxycholate, cholate, Cetri-51

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Comparative effects, in vitro, of various detergents on liver glucose-6-phosphate phosphohydrolase, inorganic pyrophosphate-glucose phosphotransferase, and acid inorganic pyrophosphatase activities

Cited by 32 publications

References 11 publications

Purification, characterization and initial rate kinetics of acyl-phosphate-hexose phosphotransferase from Aerobacter aerogenes

Purification, characterization and initial rate kinetics of acyl-phosphate-hexose phosphotransferase from Aerobacter aerogenes

Glucose-6-phosphatase

A new, sensitive determination of phosphate

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