Native bovine serum albumin (BSA) is a 66 kDa protein, which belongs to the family of serum albumin. It consists of three domains (I, II and III) and is the major protein found in circulatory system. Native BSA is an α-helical, globular and non-glycosylated protein, with 17-disulfide bonds.
Acetylation of bovine serum albumin modifies various residues, most notably lysine (Lys), and also serine (Ser) and threonine (Thr) to lesser extents. MALDI-TOF mass spectrometry studies on acetylated BSA have indicated a MW value about 3000 Da higher compared to native BSA (Ostatná, V. et al., J. Electroanalytical Chem., 821, 97-103 (2018)).. Acetylation of BSA also modifies parallel amino acid residues in any trace contaminating nucleases in the BSA, which inactivates that trace nuclease content. Thus acetylated BSA can be used in molecular biology applications where trace nuclease activity must be minimized.