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PUBLICATIONS

Comparison of the Unfolding Properties of Recombinant Human Serum Albumin Products

Published

Author(s)

Brian E. Lang, Kenneth D. Cole

Abstract

We have used Differential scanning calorimetry (DSC) to determine the unfolding properties of human serum albumin (HSA) from pooled blood and from several recombinant sources. The melting temperature, Tm, for the unfolding of HSA varied from 62 °C to 75 °C, with the reverence value of Tm of 68 °C as determined from the pooled HSA sample. We have looked at the effects of heat pasteurization and on defatting techniques on the transition temperature. We have also examined some of the effects of fatty acids on the individual domains of HSA and have how the addition of fatty acids helps to stabilize the domain interactions.
Citation
Journal of Pharmaceutical Sciences
Pub Type
Journals

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Local Download

Keywords

Human Serum Albumin, Differential Scanning Calorimetry
Biomanufacturing and Thermodynamics

Citation

Lang, B. and Cole, K. (2015), Comparison of the Unfolding Properties of Recombinant Human Serum Albumin Products, Journal of Pharmaceutical Sciences, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=912528 (Accessed October 2, 2025)

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Created January 15, 2015, Updated March 17, 2017
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