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Photon correlation spectroscopy of human IgG.

T Jøssang1, J Feder, E Rosenqvist

  • 1Institute of Physics, University of Oslo, Blindern, Norway.

Journal of Protein Chemistry
|April 1, 1988
PubMed
Summary
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Photon-correlation spectroscopy measured human immunoglobulin G (IgG) diffusion, revealing pH-dependent size changes. Monomeric IgG diffusion coefficients and hydrodynamic radii were determined, with ferritin proposed as a light-scattering standard.

Area of Science:

  • Biophysics
  • Physical Chemistry

Background:

  • Understanding protein behavior in solution is crucial for biological and pharmaceutical applications.
  • Accurate measurement of protein size and interactions informs drug development and diagnostics.

Purpose of the Study:

  • To determine the translational diffusion coefficient of monomeric human immunoglobulin G (IgG) across varying pH and concentrations.
  • To investigate the effect of pH on IgG's hydrodynamic radius and solution electrostatic interactions.
  • To evaluate monomeric horse spleen ferritin as a reference standard for light-scattering studies.

Main Methods:

  • Photon-correlation spectroscopy (PCS) was employed to measure diffusion coefficients.
  • Hydrodynamic radius was calculated from diffusion coefficients using established methods.

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  • Light-scattering principles were applied for size determination.

    • Main Results:

    • Monomeric IgG diffusion coefficient (D020,w) at pH 7.6 is 3.89 x 10(-7) cm2/sec, corresponding to a hydrodynamic radius (R) of 55.1 ± 0.3 Å.
    • Increasing pH to 8.9 caused a slight expansion in IgG's hydrodynamic radius (3.5% increase).
    • Dimeric IgG diffusion coefficient was 2.81 x 10(-7) ± 0.04 cm2/sec, with a hydrodynamic radius of 75 Å.
    • Monomeric horse spleen ferritin (R = 6.9 ± 0.1 nm) was confirmed as a stable and suitable reference standard for light-scattering.

    Conclusions:

    • The translational diffusion of monomeric IgG is sensitive to pH changes, indicating molecular expansion at higher pH.
    • Solution electrostatic effects influence IgG diffusion, with negligible long-range repulsive interactions observed in the buffer.
    • Ferritin serves as a reliable standard for light-scattering measurements of proteins in the 5-10 nm size range.