Nachweis von Konformationsisomeren im Hamoglobin(III) von Chironomus th. thummi mit Hilfe der Elektronen-Spin-Resonanz
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1970.tb01000.x/fullpdf
Reference29 articles.
1. Die O2-Bindungseigenschaften einiger Larvalhamoglobine von Chironomus th. thummi
2. Studies on the Relations between Molecular and Functional Properties of Hemoglobin
3. ESR- und CD-Spektren von pH-abhangigen Konformationsisomeren des Hamoglobin(III)
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2. Proton nuclear magnetic resonance study of the solution distal histidine orientation in monomeric Chironomus thummi thummi cyanomet hemoglobins;Journal of Molecular Biology;1991-10
3. Resonance Raman investigation of CO-ligated monomeric insect hemoglobins. Direct evidence for reciprocal changes in iron-axial ligand bonds induced by allosteric transitions.;Journal of Biological Chemistry;1986-07
4. Mechanism of the control of dioxygen binding in a dimeric cobalt-substituted insect hemoglobin. Resonance Raman evidence for cobalt - axial-ligand bond changes;European Journal of Biochemistry;1986-06
5. Non-equilibrium state of a monomeric insect haemoglobin induced by γ-irradiation and detected by Mössbauer spectroscopy;FEBS Letters;1985-07-08
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