Thermodynamic stability and formation of aggregates of human immunoglobulin G characterised by differential scanning calorimetry and dynamic light scattering
Thermodynamic stability and formation of aggregates of human immunoglobulin G characterised by differential scanning calorimetry and dynamic light scattering
Engineering Village 2
2006 Elsevier Inc
Accession number: 8880059
Title: Thermodynamic stability and formation of aggregates of human immunoglobulin G characterised by differential scanning calorimetry and dynamic light scattering
Authors: Jungbauer, A.1 ; Ahrer, K.1 ; Buchacher, A.; Iberer, G.
Author affiliation: 1 Dept. of Biotechnol., Univ. of Natural Resources & Appl. Life Sci., Vienna, Austria
Serial title: Journal of Biochemical and Biophysical Methods
Abbreviated serial title: J. Biochem. Biophys. Methods (Netherlands)
Volume: 66
Issue: 1-3
Publication date: 31 March 2006
Pages: 73-86
Language: English
ISSN: 0165-022X
CODEN: JBBMDG
Document type: Journal article (JA)
Publisher: Elsevier
Country of publication: Netherlands
Material Identity Number: J322-2006-001
Abstract: The final process step of polyclonal human immunoglobulin G is formulation with agents such as sugars, polyols, amino acid and salts. Often the most stable formulations were empirically identified. Physicochemical methods, such as differential scanning calorimetry and dynamic light scattering, provide a deeper insight on the biophysical properties of such a protein solution. The combination of these methods proved to be sensitive enough to detect fine differences in the properties relevant for the development of stable protein solutions. The influence of additives, such as maltose and glycine in combination with water or low concentrations of salts, on human immunoglobulin preparations was analysed. Differential scanning calorimetry illustrated that 0.2 M glycine had better stabilising effects compared to 10% maltose. Dynamic light scattering and differential scanning calorimetry revealed that solutions preventing aggregation were not optimal in terms of thermodynamic stability. Aggregation was minimised with increasing ionic strength, shown by dynamic light scattering, whereas thermodynamic stability for heat sensitive parts of human immunoglobulin G, analysed with differential scanning calorimetry, was decreased. [All rights reserved Elsevier]
Number of references: 35
Inspec controlled terms: aggregation - biochemistry - biological specimen preparation - biothermics - differential scanning calorimetry - light scattering - molecular biophysics - proteins - thermal stability
Uncontrolled terms: thermodynamic stability - aggregate formation - polyclonal human immunoglobulin G - differential scanning calorimetry - dynamic light scattering - physicochemical methods - protein solution - maltose - glycine - water - low salt concentrations - ionic strength
Inspec classification codes: A8780 Biophysical instrumentation and techniques - A8715D Physical chemistry of biomolecular solutions; condensed states - A8716 Biothermics - A8715M Interactions with radiations at the biomolecular level - A8270 Disperse systems
Treatment: Practical (PRA); Experimental (EXP)
Discipline: Physics (A)
DOI: 10.1016/j.jbbm.2005.12.003
Database: Inspec
Copyright 2006, The Institution of Engineering and Technology
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