Copper binding selectivity of N- and C-sites in serum (human)- and ovo-transferrin
- 15 August 1996
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1296 (1) , 103-111
- https://doi.org/10.1016/0167-4838(96)00058-1
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: Implications for transferrin iron releaseBiochemistry, 1993
- Transferrin: the role of conformational changes in iron removal by chelatorsJournal of the American Chemical Society, 1993
- Metal-induced Conformational Changes in TransferrinsJournal of Molecular Biology, 1993
- Anion binding by human lactoferrin: results from crystallographic and physicochemical studiesBiochemistry, 1992
- Metal substitution in transferrins: the crystal structure of human copper-lactoferrin at 2.1-.ANG. resolutionBiochemistry, 1992
- Preliminary crystallographic studies of copper(II)- and oxalate-substituted human lactoferrinJournal of Molecular Biology, 1991
- Apolactoferrin structure demonstrates ligand-induced conformational change in transferrinsNature, 1990
- Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2·8 Å resolutionJournal of Molecular Biology, 1989
- Molecular structure of serum transferrin at 3.3-.ANG. resolutionBiochemistry, 1988
- The effect of salts on the kinetics of iron release from N-terminal and C-terminal monoferrictransferrinsBiochemical and Biophysical Research Communications, 1981