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Structural and immunologic characterization of bovine, horse, and rabbit serum albumins.

Molecular immunology (2012-06-09)
Karolina A Majorek, Przemyslaw J Porebski, Arjun Dayal, Matthew D Zimmerman, Kamila Jablonska, Alan J Stewart, Maksymilian Chruszcz, Wladek Minor
ABSTRACT

Serum albumin (SA) is the most abundant plasma protein in mammals. SA is a multifunctional protein with extraordinary ligand binding capacity, making it a transporter molecule for a diverse range of metabolites, drugs, nutrients, metals and other molecules. Due to its ligand binding properties, albumins have wide clinical, pharmaceutical, and biochemical applications. Albumins are also allergenic, and exhibit a high degree of cross-reactivity due to significant sequence and structure similarity of SAs from different organisms. Here we present crystal structures of albumins from cattle (BSA), horse (ESA) and rabbit (RSA) sera. The structural data are correlated with the results of immunological studies of SAs. We also analyze the conservation or divergence of structures and sequences of SAs in the context of their potential allergenicity and cross-reactivity. In addition, we identified a previously uncharacterized ligand binding site in the structure of RSA, and calcium binding sites in the structure of BSA, which is the first serum albumin structure to contain metal ions.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Bovine Serum Albumin solution, 30% in saline, fatty acid free, aseptically filled
Sigma-Aldrich
Bovine Serum Albumin, lyophilized powder, protease, essentially free, ≥98% (agarose gel electrophoresis)
Sigma-Aldrich
Albumin, Monomer bovine, Monomer ≥97 %
Sigma-Aldrich
Albumin, Acetylated from bovine serum, protease free, for molecular biology
Sigma-Aldrich
Bovine Serum Albumin, lyophilized powder, Essentially fatty acid free
Sigma-Aldrich
Albumin from rabbit serum, lyophilized powder, essentially globulin free, ≥99% (agarose gel electrophoresis)
Sigma-Aldrich
Albumin, lactosyl bovine, lyophilized powder

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