The formation of iron-binding fragments of hen ovotransferrin by limited proteolysis
Author:
- 1 September 1974
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 141 (3) , 745-752
Abstract
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.Keywords
This publication has 31 references indexed in Scilit:
- Single-chain nature of human serum transferrinBiochemistry, 1970
- The amino acid sequence of cysteic acid-containing peptides from performic acid-oxidized ovotransferrinBiochemical Journal, 1970
- Ultraviolet difference spectral studies of conalbumin complexes with transition metal ionsBiochemistry, 1969
- Citrate-mediated exchange of Fe3+ among transferrin moleculesBiochemical and Biophysical Research Communications, 1968
- The isoelectric fractionation of hen's-egg ovotransferrinBiochemical Journal, 1968
- A comparison of glycopeptides from the ovotransferrin and serum transferrin of the henBiochemical Journal, 1968
- An Electron Paramagnetic Resonance Study of the Iron and Copper Complexes of TransferrinJournal of Biological Chemistry, 1968
- Physical evidence for transferrins as single polypeptide chainsBiochemistry, 1968
- Estimation of the molecular weights of proteins by Sephadex gel-filtrationBiochemical Journal, 1964
- The determination of glucosamine and galactosamineBiochemical Journal, 1955