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.
Original language | English |
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Pages (from-to) | 367-371 |
Number of pages | 5 |
Journal | European Biophysics Journal |
Volume | 44 |
Issue number | 5 |
DOIs | |
Publication status | Published - 15 Jul 2015 |