Abstract
Chromium (III)-albumin complexes that have allergenic properties and induce contact dermatitis are aggregated in solution. This is shown by small-angle X-ray scattering of Cr(III)-albumin solutions at 21°C in a Tris-HCl buffer of pH=7.40.
At high concentrations of Cr(III), albumin appears to aggregate to an average molecular weight of an octamer, with an average gyration radius of 116 Å. At low concentration of Cr(III), dimers and also some higher polymers form with an average molecular weight of 135,000 and an average radius of gyration of 57 Å.
Analysis of the shapes of the Cr(III)-albumin complexes indicate that they are more elongated than albumin, suggesting that, in the presence of Cr(III), the albumin molecules associate sideways with an expansion mainly of the largest axis.
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Österberg, R., Sjöberg, B. & Persson, D. Cr(III)-Induced polymerization of human albumin. Biol Trace Elem Res 3, 157–167 (1981). https://doi.org/10.1007/BF02990114
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DOI: https://doi.org/10.1007/BF02990114
Index Entries
- Chromium contact dermatitis
- chromium(III)
- human serum albumin
- small-angle X-ray scattering
- molecular weight, of human albumin
- radius of gyration, of human albumin, weighted least-squares analysis, of albumin polymerization
- distance distribution function, of human albumins
- polymerization, of human albumins
- shape analysis, of polymerized albumin