title: The aggregation of "native" human serum albumin.
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.
authors.affiliation: Research School of Chemistry, Australian National University, Canberra, Australia, jww@rsc.anu.edu.au.
authors.forename: John
authors.initials: J
authors.lastname: White
authors.forename: David
authors.initials: D
authors.lastname: Heß
authors.forename: Jared
authors.initials: J
authors.lastname: Raynes
authors.forename: Valerie
authors.initials: V
authors.lastname: Laux
authors.forename: Michael
authors.initials: M
authors.lastname: Haertlein
authors.forename: Trevor
authors.initials: T
authors.lastname: Forsyth
authors.forename: Anithahini
authors.initials: A
authors.lastname: Jeyasingham
mesh_terms: D006801:Humans; D066329:Protein Aggregates; D011994:Recombinant Proteins / Q000737:chemistry; D012709:Serum Albumin / Q000737:chemistry*
chemical_list: D066329:Protein Aggregates; D011994:Recombinant Proteins; D012709:Serum Albumin