A variant of human transferrin with abnormal properties.
Screening of human serum samples by polyacrylamide-gel electrophoresis in the presence of 6 M-urea revealed an individual who is heterozygous for a variant transferrin. The variant transferrin is able to bind two atoms of iron, but the iron in the C-terminal binding site is bound abnormally, as judged by its spectral properties, and is dissociated from the protein on electrophoresis in the presence of 6 M-urea. The iron-free C-terminal domain of the variant protein is less stable than normal to thermal and urea denaturation. Structural changes in the variant protein have not yet been characterized.
D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006579:Heterozygote; D006801:Humans; D007501:Iron / Q000378:metabolism*; D013053:Spectrophotometry; D014168:Transferrin / Q000378:metabolism*; D014357:Trypsin / Q000494:pharmacology; D014508:Urea
D000596:Amino Acids; D014168:Transferrin; D014508:Urea; D007501:Iron; D014357:Trypsin