Fluorescence and kinetic properties of Ru(III) (NH3)5 modified transferrin
- 1 January 1991
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1076 (2), 252-258
- https://doi.org/10.1016/0167-4838(91)90275-5
Abstract
No abstract availableThis publication has 23 references indexed in Scilit:
- Molecular structure of serum transferrin at 3.3-.ANG. resolutionBiochemistry, 1988
- Effects of ionic strength on iron removal from the monoferric transferrinsInorganic Chemistry, 1988
- The effects of salts and amino group modification on the iron binding domains of transferrinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Iron uptake and utilization by mammalian cells. I: Cellular uptake of transferrin and ironTrends in Biochemical Sciences, 1983
- Oxidation-reduction catalytic activity of a pentaammineruthenium(III) derivative of sperm whale myoglobinJournal of the American Chemical Society, 1983
- Interresidue distance measurements in proteins Fluorescent energy transfer between tryptophans and a Ru(III)(NH3)5-histidine complex in α-lytic protease and lysozymeBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- The influence of pH on the equilibrium distribution of iron between the metal-binding sites of human transferrinBiochemical Journal, 1981
- Synthesis of pentaammineruthenium-histidine complexes in ribonuclease AJournal of the American Chemical Society, 1978
- Nitrogen-carbon linkage isomerism of histidine in ruthenium ammine complexesBioinorganic Chemistry, 1973
- Properties and reactions of ruthenium(II) amine complexesCoordination Chemistry Reviews, 1970