Comparison of bovine serum transferrin A and D2. I. Amino acid residue differences.
A comparison is made of single components of the homozygous variants A and D2 of bovine serum transferrin by tryptic, chymotryptic and cyanogen bromide digestion. It is concluded that there are three substitutions A:D2-Glu:Asp, Lys:Arg and Asp:Gly. In the light of the recent work of Brock et al. (1980) it is concluded that all three substitutions occur in the C-terminal sequence of the chain. By homology with the sequence of human serum transferrin (MacGillivray et al., 1982) the Lys:Arg and Asp:Gly substitutions probably occur at residues 527 and 446, respectively, from the N-terminus. The Asp:Gly substitution is considered more likely than our earlier conclusion (Maeda, McKenzie & Shaw, 1977) that there is a deletion in the chain of D2 (A:D2, Asp:--). The location of the Glu:Asp substitution is not known.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle / Q000097:blood* / Q000235:genetics; D014644:Genetic Variation; D006720:Homozygote; D010446:Peptide Fragments / Q000302:isolation & purification; D014168:Transferrin / Q000235:genetics*
D000596:Amino Acids; D010446:Peptide Fragments; D014168:Transferrin