Journal article
Heme-apoprotein interaction in the modified oxyhemoglobin-bis(N-maleimidomethyl)ether and in oxyghemoglobin at high Cl super(-) concentration detected by resonance Raman scattering
Biochimica et biophysica acta, Protein structure and molecular enzymology, Vol.830(3)
01 Jan 1985
Abstract
The dispersion of the depolarization ratio of oxidation and spin-marker lines of oxyhemoglobin-bis(N-maleimidomethyl)ether and oxyhemoglobin at high Cl super(-) concentration (1 M) have been examined for different pH values in the neutral and alkaline regions. The oxidation marker line at 1375 cm super(-1) shows no pH-dependence in the physiological region for oxyHb-bis(N-maleimidomethyl)ether and a comparatively small variation for oxyHb at a Cl super(-) concentration higher than 0.4 M. The spin-marker line at 1638 cm super(-1) exhibits a strong pH-dependence of depolarization ratio for high Cl super(-) concentration, but a minor pH-induced variation for oxyHb-bis(N-maleimidomethyl)ether.
Metrics
2 Record Views
Details
- Title
- Heme-apoprotein interaction in the modified oxyhemoglobin-bis(N-maleimidomethyl)ether and in oxyghemoglobin at high Cl super(-) concentration detected by resonance Raman scattering
- Creators
- D WedekindR Schweitzer-StennerW Dreybrodt
- Publication Details
- Biochimica et biophysica acta, Protein structure and molecular enzymology, Vol.830(3)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Identifiers
- 991019196664104721