The formation of iron-binding fragments of hen ovotransferrin by limited proteolysis.
1. Iron was added to hen ovotransferrin to 30% saturation and the protein was digested with trypsin or chymotrypsin. 2. Iron-binding fragments were isolated. They carried one atom of iron/mol (mol.wt. 35000) and consisted of a single polypeptide chain derived from the N-terminal half of the protein. Carbohydrate was not present. 3. The fragments were able to bind a variety of metals and to donate iron to reticulocytes.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002645:Chickens; D002918:Chymotrypsin; D004592:Electrophoresis, Starch Gel; D006868:Hydrolysis; D007501:Iron / Q000378:metabolism*; D007504:Iron Radioisotopes; D007525:Isoelectric Focusing; D008970:Molecular Weight; D009942:Organometallic Compounds; D010446:Peptide Fragments / Q000032:analysis; D011485:Protein Binding; D012156:Reticulocytes / Q000378:metabolism; D014168:Transferrin / Q000378:metabolism*; D014357:Trypsin
D000596:Amino Acids; D007504:Iron Radioisotopes; D009942:Organometallic Compounds; D010446:Peptide Fragments; D014168:Transferrin; D007501:Iron; D002918:Chymotrypsin; D014357:Trypsin