Subunits of Human Transferrin.

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Abstract
Evidence for a subunit structure was obtained by physical and chemical studies of reduced and alkylated or performic acid oxidized human transferrin. The molecular weights of the subunits were estimated between 39,400 and 44,000 by sedimentation and diffusion and by the approach to sedimentation equilibrium method. The sedimentation coefficient decreased from 5 S to 1.2 S after reduction and alkylation in 8 [image] urea. Fingerprinting patterns of trypsin digested material showed 34-38 ninhydrin positive spots; approximately half the number of peptides expected from the arginine and lysine content of native transferrin. An identical fingerprint developed by the chlorine-iodine reaction revealed an additional peptide from which no N-terminal amino acid could be obtained.