Effect of different agents on GDH aggregation.

<p>The initial parts of the dependences of the light scattering intensity on temperature for aggregation of GDH (0.12 mg/ml) in the presence of the following agents: (1) control; (2) 0.2 mM NADH; (3) 50 mM L-glutamate; (4) 0.2 mM NADH+0.5 mM ADP; (5) 50 mM L-leucine and (6) 0.5 mM ADP. Points are the experimental data. The solid curves were calculated from Eq. (4).</p

Effect of ADP on GDH aggregation.

<p>(<b>A</b>) The initial parts of the dependences of the light scattering intensity on temperature for aggregation of GDH (0.16 mg/ml) in the presence of the following concentrations of ADP: (1) 0, (2) 0.05, (3) 0.1, (4) 0.5 and (6) 2 mM. (<b>B</b> and <b>C</b>) The dependences of parameters <i>T</i>₀ and <i>K</i>_agg calculated from Eq. (4) on the ADP concentration, respectively. The solid curve in panel <b>C</b> was calculated from Eq. (10) at <i>K</i>_diss = 0.52 mM.</p

The relationships between the increment of the light scattering intensity accompanying Ph<i>b</i> aggregation and the portion of the denatured Ph<i>b</i> (γ_den) calculated from the DSC data.

<p>Ph<i>b</i> concentrations were as follows: (1) 0.95 and (2) 1.9 mg/ml. The inset shows the initial parts of the curves. Points are the experimental data. The solid curves are calculated from Eq. (6).</p

Estimation of the size of the protein aggregates formed in the course of CK aggregation registered in the regime of heating at the rate of 1°C/min (30 mM Hepes–NaOH buffer, pH 8.0, containing 0.1 M NaCl).

<p>(<b>A</b>) The initial parts of the dependences of the hydrodynamic radius (<i>R</i>_h) of the protein aggregates on temperature obtained at the following CK concentrations: (1) 0.1, (2) 0.75 and (3) 1.5 mg/ml. (<b>B</b> and <b>C</b>) The dependences of parameter <i>R</i>_h,0 and the reciprocal value of parameter Δ<i>T</i>_2R calculated from Eq. (9) on the GAPDH concentration, respectively.</p

Analysis of the kinetics of GAPDH aggregation registered in the regime of heating at the rate of 1°C/min (10 mM Na-phosphate buffer, pH 7.5, containing 0.1 M NaCl).

<p>(<b>A</b>) The initial parts of the dependences of the light scattering intensity on temperature obtained at the following concentrations of GAPDH: (1) 0.1, (2) 0.75 and (3) 1.5 mg/ml. Points are the experimental data. The solid curves were calculated from Eq. (4). (<b>B</b> and <b>C</b>) The dependences of parameters <i>T</i>₀ and <i>K</i>_agg calculated from Eq. (4) on the GAPDH concentration, respectively.</p

Estimation of the size of the protein aggregates formed in the course of GAPDH aggregation registered in the regime of heating at the rate of 1°C/min (10 mM Na-phosphate buffer, pH 7.5, containing 0.1 M NaCl).

<p>(<b>A</b>) The initial parts of the dependences of the hydrodynamic radius (<i>R</i>_h) of the protein aggregates on temperature obtained at the following GAPDH concentrations: (1) 0.1, (2) 0.25, (3) 0.5 and (4) 1.5 mg/ml. (<b>B</b> and <b>C</b>) The dependences of parameter <i>R</i>_h,0 and the reciprocal value of parameter Δ<i>T</i>_2R calculated from Eq. (8) on the GAPDH concentration, respectively.</p

Thermal denaturation of Ph<i>b</i> (0.08 M Hepes-buffer, pH 6.8, containing 0.1 M NaCl).

<p>The dependences of the excess heat capacity () on temperature, obtained at the following concentrations of Ph<i>b</i>: (1) 0.95 and (2) 1.9 mg/ml. was calculated per dimer of Ph<i>b</i> with the molecular mass of 194.8 kDa. The heating rate was 1°C/min.</p

Parameters of aggregation of GDH (0.12 mg/ml) in the presence of different ligands (0.1 M Na-phosphate buffer, pH 7.6).

<p>Parameters of aggregation of GDH (0.12 mg/ml) in the presence of different ligands (0.1 M Na-phosphate buffer, pH 7.6).</p

Effect of different agents on Ph<i>b</i> aggregation.

<p>The initial parts of the dependences of the light scattering intensity on temperature for aggregation of Ph<i>b</i> (0.5 mg/ml) in the presence of the following agents: (1) control, (2) 1 mM AMP, (3) 0.19 M HP-β-CD, (4) 1 M TMAO and (5) α-crystallin at the concentration of 1 mg/ml. Points are the experimental data. The solid curves were calculated from Eq. (4).</p

Estimation of the size of the protein aggregates formed in the course of GDH aggregation registered in the regime of heating at the rate of 1°C/min (0.1 M Na-phosphate buffer, pH 7.6).

<p>(<b>A</b>) The initial parts of the dependences of the hydrodynamic radius (<i>R</i>h) of the protein aggregates on temperature obtained at the following GDH concentrations: (1) 0.1, (2) 0.2, (3) 0.3 and (4) 0.4 mg/ml. (<b>B</b> and <b>C</b>) The dependences of parameter <i>R</i>_h,0 and the reciprocal value of parameter Δ<i>T</i>_2R calculated from Eq. (9) on the GDH concentration, respectively.</p