Abstract
Differential scanning calorimetry (DSC) has been employed to study the thermal denaturation processes of the main protein fractions of blood serum. These processes have been compared for albumins (nondefatted (HSA) and fatty acid free (HSAf)), α,β-globulins, γ-globulins, and their mixtures in aqueous (pH 6.5) and buffer (pH 7.2) solutions. The results have indicated that α,β-globulins inhibit γ-globulins’ aggregation in buffer solutions. The decrease of stability of HSA and HSAf aqueous solutions has been observed in the presence of γ-globulins. The mixtures of albumins and γ-globulins have revealed the tendency to ready aggregation in water. Moreover, the results have suggested that neither γ-globulins nor albumins severely change the stability of α,β-globulins.
Similar content being viewed by others
References
Almogren A, Kerr MA. Irreversible aggregation of the Fc fragment derived from polymeric but not monomeric serum IgA1—Implications in IgA-mediated disease. Mol Immunol. 2008;45:87–94.
Almogren A, Furtado PB, Sun Z, Perkins SJ, Kerr MA. Purification, properties and extended solution structure of the complex formed between human immunoglobulin A1 and human serum albumin by scattering and ultracentrifugation. J Mol Biol. 2006;356:413–31.
Hochepied T, Berger FG, Baumann H, Libert C. α-Acid glycoprotein: an acute phase protein with inflammatory and immunomodulating properties. Cytokine Growth Factor Rev. 2003;14:25–34.
Gunnarsson M, Stigbrand T, Jensen PEH. Aberrant forms of α2-macroglobulin purified from patients with multiple sclerosis. Clin Chim Acta. 2000;295:27–40.
Monaselidze J, Kalandadze Y, Topuridze I, Gadabadze M. Thermodynamic properties of serum and plasma of patients sick with cancer. High Temp High Press. 1997;29:677–81.
Garbett NC, Miller JJ, Jenson AB, Miller DM, Chaires JB. Interrogation of the plasma proteome with differential scanning calorimetry. Clin Chem. 2007;53:2012–4.
Garbett NC, Miller JJ, Jenson AB, Chaires JB. Calorimetry outside the box: a new window into the plasma proteome. Biophys J. 2008;94:1377–83.
Dàvila E, Parés D, Howell NK. Studies on plasma protein interactions in heat-induced gels by differential scanning calorimetry and FT-Raman spectroscopy. Food Hydrocoll. 2007;21:1144–52.
Cao XM, Yang X, Shi JY, Liu YW, Wang CX. The effect of glucose on bovine serum albumin denatured aggregation kinetics at high concentration the master plots method study by DSC. J Therm Anal Calorim. 2008;93:451–8.
Cao X, Wang Z, Yang X, Liu Y, Wang C. Effect of sucrose on bsa denatured aggregation at high concentration studied by the iso-conversional method and the master plots method. J Therm Anal Calorim. 2009;95:969–76.
Michnik A, Michalik K, Kluczewska A, Drzazga Z. Comparative DSC study of human and bovine serum albumin. J Therm Anal Calorim. 2006;84:113–7.
Shrake A, Finlayson JS, Ross PD. Thermal stability of human albumin measured by differential scanning calorimetry. I. Effects of caprylate and N-acetyltryptophanate. Vox Sang. 1984;47:7–18.
Khachidze DG, Monaselidze DR. Microcalorimetric study of human blood serum. Biophysics. 2000;45:320–4.
Relkin P, Kamyshny A, Magdassi S. Changes in calorimetric parameters and solvent accessibility of hydrophobic groups in native and chemically modified immunoglobulin G. J Phys Chem B. 2000;104:4980–5.
Martsev SR, Kravchuk ZI, Vlasov AP, Lyakhnovich GV. Thermodynamic and functional characterization of stable IgG conformer obtained by renaturation from a partially structured low pH-induced state. FEBS Lett. 1995;361:173–5.
Vermeer AWP, Bremer MGEG, Norde W. Structural changes of IgG induced by heat treatment and by adsorption onto a hydrophobic teflon surface studied by circular dichroizm spectroscopy. Biochim Biophys Acta. 1998;1425:1–12.
Kapłon TM, Michnik A, Drzazga Z, Richter K, Kochman M, Ożyhar A. The ro-shaped conformation of Starmaker. Biochim Biophys Acta. 2009;1794:1616–24.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Michnik, A., Drzazga, Z. Thermal denaturation of mixtures of human serum proteins. J Therm Anal Calorim 101, 513–518 (2010). https://doi.org/10.1007/s10973-010-0826-5
Published:
Issue Date:
DOI: https://doi.org/10.1007/s10973-010-0826-5