The complexation of zinc in intact human erythrocytes studied by 1H spin‐echo NMR
- 14 November 1980
- journal article
- Published by Wiley in FEBS Letters
- Vol. 121 (1), 61-64
- https://doi.org/10.1016/0014-5793(80)81267-1
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- Spin-echo Fourier transform nuclear magnetic resonance spectroscopyAnalytical Chemistry, 1979
- The incorporation of 2h‐labelled glycine into the glutathione of intact human erythrocytes studied by 1h spin‐echo fourier transform NMRFEBS Letters, 1979
- The oxygen-linked zinc-binding site of human haemoglobinBiochemical Journal, 1978
- Human erythrocyte metabolism studies by 1H spin echo NMRFEBS Letters, 1977
- Interaction of zinc with hemoglobin: binding of zinc and the oxygen affinityBiochemistry, 1977
- Cross correlation of titrating histidines in oxy‐ and deoxyhaemoglobin; an NMR studyFEBS Letters, 1976
- Studies on the interaction of zinc with human hemoglobinArchives of Biochemistry and Biophysics, 1974
- Nuclear magnetic resonance studies of the solution chemistry of metal complexes. IX. Binding of cadmium, zinc, lead, and mercury by glutathioneJournal of the American Chemical Society, 1973
- Effect of zinc on increasing oxygen affinity of sickle and normal red blood cellsBiochemical and Biophysical Research Communications, 1973