Dielectric properties of oxyhemoglobin and deoxyhemoglobin in aqueous solution at microwave frequencies

✍ Scribed by W. Von Casimir; N. Kaiser; F. Keilmann; A. Mayer; H. Vogel

• Publisher: Wiley (John Wiley & Sons)
• Year: 1968
• Tongue: English
• Weight: 508 KB
• Volume: 6
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.1968.360061205

✦ Synopsis

The complex dielectric constant of aqueous hemoglobin solution waa 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 waa studied. Relative measurements, with the sensitivity increased by a factor of 20, were made with alternatingly oxygenated and deoxygenated human hemoglobin solutions. The oxygenation of hemoglobin waa found to leave the hydrated molecule volume invariant within f 2 5 0 1 3 , while a shift of the relaxation wavelength of 0.0025 f 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.