Effects of organic solvents on the enzyme activity of Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase in calorimetric assays

Wiggers, Helton José; Cheleski, Juliana; Zottis, Aderson; Oliva, Glaucius; Andricopulo, Adriano D.; Montanari, Carlos Alberto

doi:10.1016/j.ab.2007.06.042

Cited by 50 publications

(34 citation statements)

References 24 publications

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“…Some authors show that in the presence of organic solvents (mono-, di-and three-valence alcohols) enzymes exhibit high stability and different substrate specificity [33][34][35][36]. Other authors have found that improving the stability of the enzyme can be achieved only at low concentrations of organic solvent [37][38][39]. By increasing the concentration of organic solvent, however, was observed inactivation [31,40], caused mainly from reversible conformational changes in the protein molecules.…”

Section: Effect Of Modified Agent On the Proprieties Of Immobilized Ementioning

confidence: 92%

Immobilization of β-galactosidase on modified polypropilene membranes

Vasileva

Iotov

Ivanov

et al. 2012

International Journal of Biological Macromolecules

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Section: Effect Of Modified Agent On the Proprieties Of Immobilized Ementioning

confidence: 92%

Immobilization of β-galactosidase on modified polypropilene membranes

Vasileva

Iotov

Ivanov

et al. 2012

International Journal of Biological Macromolecules

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“…We hypothesized that use of DMSO and glycerol might change target site preference and increase transposition activity based on the fact that these molecules can modify water structure around proteins in aqueous solution resulting in increased or decreased enzyme activity [Pasha et al, 2002;Rehan and Younus, 2006;Wiggers et al, 2007]. The use of DMSO or glycerol can change the DNA-binding specificity of some restriction enzymes [Bishop, 1979;Conlan et al, 1999;Izsvák and Duda, 1989;Tikchonenko et al, 1978].…”

Section: Discussionmentioning

confidence: 99%

“…3 D). It is known that DMSO and glycerol can modify water structure around an enzyme in aqueous solution resulting in altered enzyme activity [Pasha et al, 2002;Rehan and Younus, 2006;Wiggers et al, 2007]. Therefore, we tested transposition activity in the presence of DMSO and glycerol.…”

Section: Buffer Optimization For Improved Transposition Activitymentioning

confidence: 99%

N-Terminal Domain-Deleted Mu Transposase Exhibits Increased Transposition Activity with Low Target Site Preference in Modified Buffers

Kim¹,

Morrison²

2008

Microb Physiol

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Background: Transposition using MuA and the Mu-transposon is frequently used for insertional and deletional mutagenesis and to introduce primer sequences into DNA of unknown sequence. However, mutagenesis studies are often limited by the number of transposition events taking place within a small target sequence. Although the intrinsic target site preference of MuA is low, it nevertheless may limit the recovery of desired events. Methods: In the current study, we have compared the transposition activity of wild-type, C-terminally deleted, N-terminally deleted and both C- and N-terminally deleted MuA. Results: We found that N-terminally deleted MuA was most active with an about sevenfold increase in transposition efficiency compared to wild-type. In addition, we identified a novel reaction condition in which the transposition activity of N-terminally deleted MuA was increased about 45-fold. Conclusion: The use of the N-terminally deleted MuA with the newly established condition enhanced the relative transposition activity about 280-fold compared to that of wild-type MuA with the conventional buffer. In addition, the optimized buffer decreased the target site preference of N-terminally deleted MuA resulting in a more even distribution of integration events throughout the target gene.

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“…Although ITC measurements are usually carried out in aqueous solutions, [26,27] its use is also unproblematic with cosolvents like methanol or DMSO, [28] or with organic solvents like chloroform, [29,30] toluene, [7,29,31,32] and others. [33] Benzene, toluene, and mesitylene were used as apolar model solvents.…”

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confidence: 99%

Complexation of Phenol and Thiophenol by Amine N‐Oxides: Isothermal Titration Calorimetry and ab Initio Calculations

et al. 2010

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To develop a new solvent-impregnated resin (SIR) system for removal of phenols from water, the complex formation of dimethyldodecylamine N-oxide (DMDAO), trioctylamine N-oxide (TOAO), and tris(2-ethylhexyl)amine N-oxide (TEHAO) with phenol (PhOH) and thiophenol (PhSH) is studied. To this end we use isothermal titration calorimetry (ITC) and quantum chemical modeling (on B3LYP/6-311G(d,p)-optimized geometries: B3LYP/6-311+G(d,p), B3LYP/6-311++G(2d,2p), MP2/6-311+G(d,p), and spin component scaled (SCS) MP2/6-311+G(d,p); M06-2X/6-311+G(d,p)//M06-2X/6-311G(d,p), MP2 with an extrapolation to the complete basis set limit (MP2/CBS), as well as CBS-Q). The complexes are analyzed in terms of structural (e.g., bond lengths) and electronic elements (e.g., charges). Furthermore, complexation and solvent effects (in benzene, toluene, and mesitylene) are investigated by ITC measurements, yielding binding constants K, enthalpies ΔH(0), Gibbs fre energies ΔG(0), and entropies ΔS(0) of complex formation, and stoichiometry N. The ITC measurements revealed strong 1:1 complex formation between both DMDAO-PhOH and TOAO-PhOH. The binding constant (K=1.7-5.7×10(4) M(-1)) drops markedly when water-saturated toluene was used (K=5.8×10(3) M(-1)), and π-π interaction with the solvent is shown to be relevant. Quantum mechanical modeling confirms formation of stable 1:1 complexes with linear hydrogen bonds that weaken on attachment of electron-withdrawing groups to the amine N-oxide moiety. Modeling also showed that complexes with PhSH are much weaker than those with PhOH, and in fact too weak for ITC determination. CBS-Q incorrectly predicts equal or even higher binding enthalpies for PhSH than for PhOH, which invalidates it as a benchmark for other calculations. Data from the straightforward SCS-MP2 method without counterpoise correction show very good agreement with the MP2/CBS values.

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Effects of organic solvents on the enzyme activity of Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase in calorimetric assays

Cited by 50 publications

References 24 publications

Immobilization of β-galactosidase on modified polypropilene membranes

Immobilization of β-galactosidase on modified polypropilene membranes

N-Terminal Domain-Deleted Mu Transposase Exhibits Increased Transposition Activity with Low Target Site Preference in Modified Buffers

Complexation of Phenol and Thiophenol by Amine N‐Oxides: Isothermal Titration Calorimetry and ab Initio Calculations

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