Structure and functional properties of chemically modified horse hemoglobin. I. Determination of the functional properties.
Abstract: No abstract available
Publication Date: 1971-05-28 PubMed ID: 5104369DOI: 10.1016/0022-2836(71)90232-4Google Scholar: Lookup
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- Journal Article
Cite This Article
APA
Simon SR, Arndt DJ, Konigsberg WH.
(1971).
Structure and functional properties of chemically modified horse hemoglobin. I. Determination of the functional properties.
J Mol Biol, 58(1), 69-77.
https://doi.org/10.1016/0022-2836(71)90232-4 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Binding Sites
- Bromine
- Chemical Phenomena
- Chemistry
- Ethers
- Hemoglobins
- Horses
- Osmotic Pressure
- Oxygen / blood
- Pyrroles
Citations
This article has been cited 6 times.- Jelenc PC, Cantor CR, Simon SR. High yield photoreagents for protein crosslinking and affinity labeling. Proc Natl Acad Sci U S A 1978 Aug;75(8):3564-8.
- Alpert B, Banerjee R, Lindqvist L. The kinetics of conformational changes in hemoglobin, studied by laser photolysis. Proc Natl Acad Sci U S A 1974 Feb;71(2):558-62.
- el Naggar S, Dreybrodt W, Schweitzer-Stenner R. Haem-apoprotein interactions detected by resonance Raman scattering in Mb- and Hb-derivates lacking the saltbridge His146 beta-Asp94 beta. Eur Biophys J 1985;12(1):43-9.
- Schweitzer-Stenner R, Wedekind D, Dreybrodt W. Correspondence of the pK values of oxyHb-titration states detected by resonance Raman scattering to kinetic data of ligand dissociation and association. Biophys J 1986 May;49(5):1077-88.
- Brunzel U, Dreybrodt W, Schweitzer-Stenner R. pH-dependent absorption in the B and Q bands of oxyhemoglobin and chemically modified oxyhemoglobin (BME) at low Cl- concentrations. Biophys J 1986 May;49(5):1069-76.
- Schweitzer-Stenner R, Wedekind D, Dreybrodt W. The influence of structural variations in the F- and FG-helix of the beta-subunit modified oxyHb-NES on the heme structure detected by resonance Raman spectroscopy. Eur Biophys J 1989;17(2):87-100.
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