Brandt J, Andersson L O
Int J Pept Protein Res. 1976;8(1):33-7. doi: 10.1111/j.1399-3011.1976.tb02478.x.
Prolonged heat treatment of solutions of human serum albumin at 60 degrees C resulted in formation of one aggregate fraction and one fraction that was stable against further heat treatment. Fatty acid analyses of these fractions indicate that the heat stable fraction is formed by migration of fatty acids from the aggregating molecules to the remaining monomer thereby stabilizing the latter against heat denaturation. Disulphide and SH groups are involved in the aggregation process.
