Bovine Serum Albumin

General description
Bovine serum albumin is a model protein in various studies and is made up of 583 amino acids.[1][2] It is a water-soluble protein with a molecular weight of 66.4kDa. Six α-helices form three homologous domains of BSA. Depending on pH, it undergoes reversible conformational isomerization. The native structure of the protein becomes reactive and flexible on heating.[3] Application
Bovine Serum Albumin has been used in solution prepared for the isolation of heart mitochondria.[4] It has been used in the cytotoxicity assay buffer.[5] It has been used for the induction of protein overload nephropathy in rats.[6] Biochem/physiol Actions
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.
Preparation Note
Often referred to as Cohn fraction V; this product is prepared by a modified method of the Cohn cold ethanol fractionation method.
Serum albumin may be referred to as Fraction V. This naming convention is taken from the original Cohn method of fractionating serum proteins using cold ethanol precipitation. Serum albumin was found in the fifth ethanol fraction using Cohn′s method. Since then, the term “Fraction V” has been used by some to describe serum albumin regardless of the method of preparation. Others have used this term to describe serum albumin purified by ethanol fractionation methods that have been highly modified since the original Cohn method was described. Sigma-Aldrich manufactures and distributes serum albumins purified from a variety of primary methods including the true Cohn fractionation method, modified ethanol fractionation methods, heat shock and chromatography. Additional purification steps may include crystallization or charcoal filtration.