Some physical-chemical properties of reduced-alkylated and sulphitolysed human serum transferrins and hen's-egg conalbumin.

1. Apparently all disulphide bridges of transferrin and conalbumin were broken by reduction-alkylation, whereas sulphitolysis resulted in incomplete cleavage of disulphide bonds. 2. The molecular weights of reduced-alkylated and sulphitolysed transferrin and reduced-alkylated conalbumin were identical with those of native proteins in a number of solvents, indicating that these proteins exist as single polypeptide chains. 3. Viscosity studies indicated that reduced-alkylated transferrin possesses a partially ordered structure in 0-4m-urea, assumes a random-coil configuration in 6m-urea with a molecular weight of 84000 and is partially aggregated in 8m-urea.