Iron-binding fragments from the N-terminal and C-terminal regions of human lactoferrin.
Digestion of lactoferrin with pepsin at pH3.0 gave an iron-binding half-molecule that represents the C-terminal part of the native protein. Tryptic or chymotryptic digestion of 30%-iron-saturated lactoferrin yielded the N- and C-terminal half molecules, which could be separated by DEAE-Sephadex chromatography. The N- and C-terminal fragments did not show any immunological cross-reaction. The carbohydrate of lactoferrin was distributed equally between the two fragments.
D000596:Amino Acids / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D006801:Humans; D007501:Iron; D007781:Lactoferrin / Q000032:analysis; D007782:Lactoglobulins / Q000032:analysis; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D011485:Protein Binding; D014357:Trypsin
D000596:Amino Acids; D002241:Carbohydrates; D007782:Lactoglobulins; D010446:Peptide Fragments; D007501:Iron; D007781:Lactoferrin; D014357:Trypsin