Characterization and Comparison of Human, Bovine, Sheep, Pig, Goat and Rat Serum Albumins by FT-IR Spectroscopy and Sequence Comparison

Sarah F. Garelick¹, Rina K. Dukor², and Teresa E. Thornton¹

1Oxbridge Academy, 3151 North Military Trail, West Palm Beach, Florida, 33409, USA; 2BioTools, Inc. 17546 Bee Line Hwy, Jupiter, Florida, 33458, USA

The determination of serum albumin (SA) structure transferability to identify the similarities among species can be applied in the clinical, pharmaceutical, and biochemical fields. As the most prevalent plasma protein in mammals, this protein serves as a transporter for a diverse range of metabolites, drugs, nutrients, and molecules. Its binding properties and three-dimensional structure functions as a transporter in all animals; and, despite having different amino acid sequences, mammalian SAs have shown significant homologies. However, it is the distinguishability of different SA sequences that causes them to function as allergens. This study employed sequence homology algorithms to determine the percent identity between different species. FT-IR spectroscopy was then used to characterize and compare the secondary structures of human, bovine, sheep, pig, goat and rat serum albumins in water adjusted to a pH of 6.5. Results demonstrate the secondary structural differences between mammalian serum albumins were less than 1%, noting transferability of structural studies between different species.