Preparation methods have a large influence on the folding and oligomerization behaviour of proteins in solution. In an experiment carried out by Anton Paar, bovine serum albumin (BSA) dissolved in deionized water (BSA-H2O) was compared to BSA re-suspended in the isotonic buffer PBS (BSA-PBS). Particle size results suggested that BSA-H20 had suffered denaturation and/or aggregation, while BSA-PBS primarily consisted in native BSA dimers. Molecular mass measurements performed on BSA-H20 returned erroneous results due to the multimodal nature of the sample, while those performed on BSA-PBS displayed the expected molecular mass of dimeric BSA.
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