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Dielectric properties of oxyhemoglobin and deoxyhemoglobin in aqueous solution at microwave frequencies
Author(s) -
Von Casimir W.,
Kaiser N.,
Keilmann F.,
Mayer A.,
Vogel H.
Publication year - 1968
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1968.360061205
Subject(s) - hemoglobin , chemistry , aqueous solution , dielectric , analytical chemistry (journal) , microwave , relaxation (psychology) , wavelength , oxygenation , nuclear magnetic resonance , deoxygenated hemoglobin , oxygen , chromatography , optics , biochemistry , materials science , organic chemistry , psychology , social psychology , ecology , quantum mechanics , biology , physics , optoelectronics
The complex dielectric constant of aqueous hemoglobin solution was measured at 9.5 GHz. A microwave technique allowing phase and attenuation settings with an accuracy of 0.3° and 0.03 db was used. The shift of the relaxation wavelength and the hydration values of horse hemoglobin were determined for native and lyophilized hemoglobin solution and erythrocytes suspensions as well. The isotope effect of light and heavy water on these parameters was detected. The influence of buffers was studied. Relative measurements, with the sensitivity increased by a factor of 20, were made with alternating oxygenated and deoxygenated human hemoglobin solutions. The oxygenation of hemoglobin was found to leave the hydrated molecule volume invariant within ±250 Å 3 , while a shift of the relaxation wavelength of 0.0025 ± 0.0015 cm occurs for a hemoglobin concentration of 107 g/l. The results are discussed in terms of the structure and function interrelationship of hemoglobin and the current picture of water structure.