Characterization of monoferric fragments obtained by tryptic cleavage of bovine transferrin.
1. The electrophoretically fast (F) and slow (S) fragments obtained by tryptic cleavage of bovine iron-saturated transferrin differed in carbohydrate content and peptide 'maps'. 2. A fragment capable of binding one Fe3+ ion per molecule was isolated after brief tryptic digestion of bovine apotransferrin and shown closely to resemble the S fragment obtained from the iron-saturated protein. 3. Fragments F and S are probably derived from the N- and C-terminal halves of the transferrin molecule respectively. 4. Bovine transferrin could donate iron to rabbit reticulocytes, but the monoferric fragments possessed little iron-donating ability.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D007501:Iron / Q000378:metabolism; D008623:Mercaptoethanol; D010446:Peptide Fragments / Q000032:analysis; D012156:Reticulocytes / Q000378:metabolism; D014168:Transferrin / Q000032:analysis* / Q000378:metabolism; D014357:Trypsin
D000596:Amino Acids; D002241:Carbohydrates; D010446:Peptide Fragments; D014168:Transferrin; D008623:Mercaptoethanol; D007501:Iron; D014357:Trypsin