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

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Abstract
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.