A test to evaluate the effect of individual components of ethylene glycol bis(β-aminoethyl ether)-N,N,N′,N′-tetraacetic acid buffers on enzymatic activity

Vidal, Hubert; St-Denis, Jean-François; Painchaud, Edith; Larue, M.; Werve, Gérald van de

doi:10.1016/0003-2697(91)90053-v

Cited by 2 publications

(3 citation statements)

References 7 publications

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“…Presumably, mannose produced from M6P by histone II-A-treated microsomes is released directly in the extravesicular medium. Figure 3 shows that increasing concentrations of EGTA (0.1-25 mM) have no effect on G6Pase or M6Pase activities in untreated microsomes, as we have shown previously [17,18], but almost completely reversed the stimulatory effect of histone 11-A on both G6Pase and M6Pase. Similar results were obtained when EDTA was used instead of EGTA (not shown).…”

supporting

confidence: 64%

Histone II-A stimulates glucose-6-phosphatase and reveals mannose-6-phosphatase activities without permeabilization of liver microsomes

St-Denis

Annabi

Khoury

et al. 1995

Biochemical Journal

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The effect of histone II-A on glucose-6-phosphatase and mannose-6-phosphatase activities was investigated in relation to microsomal membrane permeability. It was found that glucose-6-phosphatase activity in histone II-A-pretreated liver microsomes was stimulated to the same extent as in detergent-permeabilized microsomes, and that the substrate specificity of the enzyme for glucose 6-phosphate was lost in histone II-A-pretreated microsomes, as [U-14C]glucose-6-phosphate hydrolysis was inhibited by mannose 6-phosphate and [U-14C]mannose 6-phosphate hydrolysis was increased. The accumulation of [U-14C]glucose from [U-14C]glucose 6-phosphate into untreated microsomes was completely abolished in detergent-treated vesicles, but was increased in histone II-A-treated microsomes, accounting for the increased glucose-6-phosphatase activity, and demonstrating that the microsomal membrane was still intact. The stimulation of glucose-6-phosphatase and mannose-6-phosphatase activities by histone II-A was found to be reversed by EGTA. It is concluded that the effects of histone II-A on glucose-6-phosphatase and mannose-6-phosphatase are not caused by the permeabilization of the microsomal membrane. The measurement of mannose-6-phosphatase latency to evaluate the intactness of the vesicles is therefore inappropriate.

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supporting

confidence: 64%

Histone II-A stimulates glucose-6-phosphatase and reveals mannose-6-phosphatase activities without permeabilization of liver microsomes

St-Denis

Annabi

Khoury

et al. 1995

Biochemical Journal

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“…2 EGTA serves as an effective inhibitor of metalloproteinases. 2,3 Organic chemists have usually attempted to understand solvent effects in terms of the solvent polarity. 4 The concept of solvent polarity is easily understood qualitatively, but it is difficult to define exactly and even more difficult to express quantitatively.…”

Section: Introductionmentioning

confidence: 99%

“…Ethylene glycol-bis(2-aminoethylether)- N , N , N ′, N ′-tetraacetic acid (EGTA) can be used as an anticoagulant when dissolved at 1 g per 100 mL of blood and chelates the calcium ion from blood . EGTA serves as an effective inhibitor of metalloproteinases. , …”

Section: Introductionmentioning

confidence: 99%

Solvatochromic Effect Studies on the Stability of Dioxovanadium(V) Complexes with Ethylene Glycol-bis(2-aminoethylether)-N,N,N′,N′-tetraacetic Acid in Different Water + Methanol Mixtures

Majlesi

Rezaienejad

2010

J. Chem. Eng. Data

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The stability constants for the reaction of dioxovanadium(V) with ethylene glycol-bis(2-aminoethylether)-N,N,N′,N′tetraacetic acid (EGTA) and the dissociation constants of EGTA were determined at 25 °C and a constant ionic strength of 0.05 mol • dm -3 sodium perchlorate in ten different compositions of water + methanol by a combination of potentiometric and UV spectrophotometric methods. The Solver, Microsoft Excel 2000 optimization package, has been used to perform nonlinear least-squares curve fitting on the basis of the Gauss-Newton method for calculation of the solvatochromic regression coefficients. Nonspecific and specific solute-solvent interactions were interpreted by correlating the equilibrium data with solvent parameters using the Kamlet-Abboud-Taft (KAT) solvatochromic equation. Finally, the influence of the solvent on the stability of the complex was discussed on the basis of the correlation results and the contribution of R (hydrogen-bond donor acidity), β (hydrogen-bond acceptor basicity), and π* (dipolarity/polarizability) parameters.

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A test to evaluate the effect of individual components of ethylene glycol bis(β-aminoethyl ether)-N,N,N′,N′-tetraacetic acid buffers on enzymatic activity

Cited by 2 publications

References 7 publications

Histone II-A stimulates glucose-6-phosphatase and reveals mannose-6-phosphatase activities without permeabilization of liver microsomes

Histone II-A stimulates glucose-6-phosphatase and reveals mannose-6-phosphatase activities without permeabilization of liver microsomes

Solvatochromic Effect Studies on the Stability of Dioxovanadium(V) Complexes with Ethylene Glycol-bis(2-aminoethylether)-N,N,N′,N′-tetraacetic Acid in Different Water + Methanol Mixtures

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