The aggregation of “native” human serum albumin

John White*, David Heß, Jared Raynes, Valerie Laux, Michael Haertlein, Trevor Forsyth, Anithahini Jeyasingham

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    6 Citations (Scopus)


    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 languageEnglish
    Pages (from-to)367-371
    Number of pages5
    JournalEuropean Biophysics Journal
    Issue number5
    Publication statusPublished - 15 Jul 2015


    Dive into the research topics of 'The aggregation of “native” human serum albumin'. Together they form a unique fingerprint.

    Cite this