A comparison of the structure and properties of human, rat and rabbit serum transferrin.
1. The chemical and physical properties of human, rat and rabbit serum transferrins were compared. 2. The proteins were found to differ in heat stability, iron release, their behaviour during electrophoresis in SDS polyacrylamide gels, and their sulphur amino acid content. 3. The results are discussed in relation to the possible role of disulphide bridges in maintaining the shape and flexibility of the three transferrins, and in their appearance during the evolution of the transferrin family.
Department of Biochemistry, London Hospital Medical College, UK.
S
S
Welch
A
A
Skinner
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001059:Apoproteins; D001665:Binding Sites; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000378:metabolism; D008970:Molecular Weight; D011489:Protein Denaturation; D011817:Rabbits; D051381:Rats; D013053:Spectrophotometry; D014168:Transferrin / Q000032:analysis / Q000378:metabolism
D000596:Amino Acids; D001059:Apoproteins; D014168:Transferrin; C028284:apotransferrin; D007501:Iron