1 Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark2 Department of Mechanical Engineering, Technical University of Denmark3 Materials and Surface Engineering, Department of Mechanical Engineering, Technical University of Denmark4 Department of Systems Biology, Technical University of Denmark5 Department of Micro- and Nanotechnology, Technical University of Denmark6 University of Southern Denmark7 Enzyme and Protein Chemistry, Department of Biotechnology and Biomedicine, Technical University of Denmark
In this study, a simple purification protocol is developed to reduce the bovine serum albumin (BSA) content in commercially available bovine submaxillary mucin (BSM). This involved purification of the BSM by one-column anion-exchange chromatography protocol resulting in BSM with greatly reduced BSA content and homogeneously distributed size, and in a high yield of 43% from BSM as received from the manufacturer. The purity and composition of commercially acquired BSM were assessed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and mass spectrometry, which verified that BSA is the most abundant nonmucinous protein component. The purification effect was evident from a significantly altered circular dichroism (CD) spectrum of BSM after anion-exchange chromatography.
Preparative Biochemistry and Biotechnology, 2015, Vol 45, Issue 1, p. 84-99