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The aggregation of 'native' human serum albumin

Authors :
David Heß
Valerie Laux
Anithahini Jeyasingham
John W. White
Trevor Forsyth
Jared K. Raynes
Michael Haertlein
Source :
European Biophysics Journal. 44:367-371
Publication Year :
2015
Publisher :
Springer Science and Business Media LLC, 2015.

Abstract

Recombinant fully deuterated, defatted human serum albumin in heavy water was found to be about 90 % aggregated before final fractionation. For comparison and to establish a datum for this isotope effect, the extent of aggregation is reported for “native” defatted and fatted human serum albumin solutions in phosphate buffered 1 mg/ml in heavy and light water at 25 °C and at 4 °C. The extent of aggregation is small over a month at these temperatures, but extensive when the solutions are subjected to repeated freeze-thawing from −18 to 25 °C in both D2O and H2O.

Details

ISSN :
14321017 and 01757571
Volume :
44
Database :
OpenAIRE
Journal :
European Biophysics Journal
Accession number :
edsair.doi.dedup.....f72971fb3dc7240f8ca93a5ed1da39c0
Full Text :
https://doi.org/10.1007/s00249-015-1030-0