Altered N----F transition in bovine serum albumin dimer and tetramer.
The monomer, dimer and tetramer of bovine serum albumin were separated by gel filtration on a Sephacryl S-300 column. Their purity was established by gel filtration, polyacrylamide gel electrophoresis and SDS polyacrylamide gel electrophoresis. These preparations were identical in bilirubin binding, cross-reactivity against anti-bovine serum albumin antiserum and UV spectral features. However, the three preparations differed in their N----F transition. The mid points of the N----F transitions for monomer, dimer and tetramer were found to be 3.75, 3.60 and 3.40 respectively. We presume that intermolecular interactions and/or alterations in the pK values of carboxyl groups are responsible for increased stability in the case of dimer and tetramer.
D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000302:isolation & purification*
D012710:Serum Albumin, Bovine