title: Aggregation of human serum albumin during a thermal viral inactivation step.
abstract: A terminal pasteurization step has been used for some plasma-derived protein products such as human serum albumin (HSA), which consists of heating the protein in solution at 60 degrees C for 10 h. Native and denaturing SDS-PAGE and dynamic light scattering were used to follow the stability of HSA during this process. It appears that a thermally unstable fraction, comprised primarily of haptoglobin, is involved in the formation of soluble aggregates of HSA. Therefore, it appears that aggregation during heat treatment is not due to conformational instability of HSA itself, but arises from unfolding of a thermally labile protein impurity. As haptoglobin aggregates, it entraps some HSA, which is present at much higher concentrations. This study emphasizes that, in a complex mixture of naturally occurring proteins, one thermally labile species can trigger aggregation of more stable proteins.
authors.affiliation: Center for Pharmaceutical Biotechnology, University of Colorado Denver Health Sciences Center, Denver, CO 80262, USA.
authors.forename: Jen-Jen
authors.initials: JJ
authors.lastname: Lin
authors.forename: Jeffrey D
authors.initials: JD
authors.lastname: Meyer
authors.forename: John F
authors.initials: JF
authors.lastname: Carpenter
authors.forename: Mark Cornell
authors.initials: MC
authors.lastname: Manning
mesh_terms: D006242:Haptoglobins / Q000737:chemistry / Q000378:metabolism; D006358:Hot Temperature; D006801:Humans; D008970:Molecular Weight; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D012995:Solubility; D013997:Time Factors; D038301:Virus Inactivation
chemical_list: D006242:Haptoglobins; D012709:Serum Albumin