Concentration and temperature dependence of viscosity in lysozyme aqueous solutions

Monkos, Karol

doi:10.1016/s0167-4838(97)00013-7

Cited by 60 publications

(66 citation statements)

References 26 publications

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“…In the present paper, the discussion of the viscosity-temperature relationship of OSA solutions is limited only to the modified Arrhenius formula. It was quite recently successfully applied to several proteins [10][11][12][13][14], and has the form:…”

Section: Resultsmentioning

confidence: 99%

“…Unfortunately, V h for OSA is unknown. However, for several proteins such calculations were made [10,11,13,14] and it was shown that the Simha factor decreases with increasing temperature. At low temperatures, the rotational Brownian motion of proteins -produced as a reaction to the random heat motions of the solvent -is negligible, and all particles should be aligned almost parallel to the direction of flow.…”

Section: Resultsmentioning

confidence: 99%

“…(7) gives S Sim = 3.76. The experimental values of S have been previously obtained for hydrated ovalbumin [13] and HSA [14], and for unhydrated BSA [10], lysozyme [11] and human IgG immunoglobulin [21]. If the hydration shell around the proteins is taken into account, small corrections in calculations are needed.…”

Section: Resultsmentioning

confidence: 99%

“…However, even for small concentrations the dependence of η sp /c versus concentration is not perfectly linear, so the linear extrapolation can give a serious error in [η] and k 1 [26]. The alternative method presented above was earlier successfully applied to several proteins [10][11][12][13][14]. It is worth noting that the numerical values of the intrinsic viscosity calculated from relation (10) at t = 25…”

Section: Resultsmentioning

confidence: 99%

“…• C ([η] = 2.66 × 10 −3 m 3 /kg for lysozyme [11] and [η] = 3.86 × 10 −3 m 3 /kg for ovalbumin [13]) agree very well with the values obtained in the traditional way at the same temperature ([η] = 2.7 × 10 −3 m 3 /kg for lysozyme and [η] = 3.9 × 10 −3 m 3 /kg for ovalbumin [27]). Moreover, the values of [η] obtained for some mammalian IgG immunoglobulins [12] lie within the range of [η] = (6-14)×10 −3 m 3 /kg reported in the literature [22].…”

Section: Resultsmentioning

confidence: 99%

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Determination of Some Hydrodynamic Parameters of Ovine Serum Albumin Solutions Using Viscometric Measurements

Monkos

2005

J Biol Phys

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Abstract. The influence of protein concentration and temperature on the viscosity of ovine serum albumin (OSA) solutions was studied. The Mooney equation and a modified Arrhenius formula were used to described the viscosity-concentration and viscosity-temperature dependence of the solutions, respectively. The effective specific volume, the activation energy and entropy of viscous flow for hydrated OSA were calculated. The axial ratio and the dimensions of the main semi-axes of hydrated OSA were established. At low concentration limit, the temperature dependence of the intrinsic viscosity and Huggins coefficient is presented. Comparison of some hydrodynamic parameters obtained for different proteins has been made.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Determination of Some Hydrodynamic Parameters of Ovine Serum Albumin Solutions Using Viscometric Measurements

Monkos

2005

J Biol Phys

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Concentration Dependence of the Viscosity of Dilute Polymer Solutions: Huggins and Schulz‐Blaschke Constants

Schöff

1999

The Wiley Database of Polymer Properties

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Structural interactions of globular proteins—Bovine serum albumin, egg albumin, and lysozyme, in aqueous medium, elucidated with molar volumes, viscosities, energy functions, and IR spectra from 293.15 to 303.15 K

Singh

2006

J of Applied Polymer Sci

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Densities (r), apparent molar volumes (V f ), viscosities (Z), and IR spectra on 0.0010-0.0018% aqueous solutions of bovine serum albumin (BSA), egg albumin (EAlb), and lysozyme at an interval of 0.0004% and at temperatures from 293.15, 298.15, and 303.15 K have obtained. The free energy (DG), entropy (DS), and enthalpy (DH) data with compositions and temperatures are calculated from the values of the flow velocity (v f ) of viscous flow, which decrease with temperature. The densities decrease with concentrations and temperatures except BSA, and the V f values slightly increase with concentrations for BSA and lysozyme, which depict structural reorientations and transition states of protein molecules with increase in viscosities and decrease in reduce viscosities. The reduce viscosities at 293.15 K for BSA, E-Alb, and lysozyme are noted positive, and for BSA and lysozyme remain positive at 298.15 and 303.15 K, whereas for E-Alb it is negative. Activation energies (E*) for lysozyme remain almost constant, and are higher than those of the BSA and E-Alb, respectively, also slightly higher E* values for the BSA than those of the E-Alb at 293.15 and 298.15, and lower than of the E-Alb at 303.15 K, are observed elucidating greater structural interactions for BSA at lower while weaker at temperatures. Stretching frequencies of amide (À ÀNHCOÀ À), À ÀNHÀ À, À ÀCO, and À ÀCHÀ À groups of proteins are noted from IR spectra with broader stretching frequencies for À ÀNHÀ À.

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Concentration and temperature dependence of viscosity in lysozyme aqueous solutions

Cited by 60 publications

References 26 publications

Determination of Some Hydrodynamic Parameters of Ovine Serum Albumin Solutions Using Viscometric Measurements

Determination of Some Hydrodynamic Parameters of Ovine Serum Albumin Solutions Using Viscometric Measurements

Concentration Dependence of the Viscosity of Dilute Polymer Solutions: Huggins and Schulz‐Blaschke Constants

Structural interactions of globular proteins—Bovine serum albumin, egg albumin, and lysozyme, in aqueous medium, elucidated with molar volumes, viscosities, energy functions, and IR spectra from 293.15 to 303.15 K

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