Bovine Serum Albumin (BSA) is a 583-residue protein consisting of three homologous all-α domains, organized in a heart-shaped structure. BSA is a globular protein that is used in numerous biochemical applications.
Bovine serum albumin (BSA) is a 583-residue protein consisting of three homologous all-α domains, organized in a heart-shaped structure. Bovine serum albumin constitutes ca. 60% of all plasma protein and binds and transports a large number of physiological and non-physiological ligands. Bovine serum albumin contains 17 disulfide bonds and one unpaired cysteine (Cys34), which facilitates dimerization and also influences higher-order association, since the rate of aggregation is slowed down if Cys34 is covalently bound to another compound. MTT assay for fibril cytotoxicity shows Bovine Serum Albumin is beneficial for cell growth irrespective of its aggregated state. Lack of cytotoxicity is confirmed by membrane permeabilization assays. In the subsequent 40 h, an increase in the viability of the treated cells of 300-400% is observed, indicating that the cells incubated with Bovine Serum Albumin achieve a higher viability than the untreated cells[1].
References:
[1]. Holm NK, et al. Aggregation and fibrillation of bovine serum albumin. Biochim Biophys Acta. 2007 Sep;1774(9):1128-38.