𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Dielectric Properties of Hemoglobin. II. Anomalous Dispersion during Oxygenation

✍ Scribed by Takashima, Shiro; Lumry, Rufus


Book ID
126063394
Publisher
American Chemical Society
Year
1958
Tongue
English
Weight
889 KB
Volume
80
Category
Article
ISSN
0002-7863

No coin nor oath required. For personal study only.


πŸ“œ SIMILAR VOLUMES


Dielectric properties and oxygenation of
✍ Maxime Hanss; Ramalprasad Banerjee πŸ“‚ Article πŸ“… 1967 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 446 KB

Dielectric properties of human and horse hemoglobin were studied at frequencies ranging from 20 kc./sec. to 7 illc./sec. The relative errors in the measurements were usually less thaii The experimental setup allowed ns variation and measurement of the degree of oxygenation of the protein and to det

Effect of oxygen binding on the dielectr
✍ Peter Schlecht; Helmut Vogel; Adalbert Mayer πŸ“‚ Article πŸ“… 1968 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 521 KB

The dielectric properties of horse hemoglobin have been investigated in the frequency range for 100 kcps to 15 Mcps at varying degrees of oxygenation. A linear dependence of the specific increment on the degree of oxygenation wae found under a variety of experimental conditions, the increment of oxy

Dielectric properties of hemoglobin and
✍ P. Schlecht; A. Mayer; G. Hettner; H. Vogel πŸ“‚ Article πŸ“… 1969 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 558 KB

Department der Technischen Hochschule Munchen, G e m n y ## Synopsis Dielectric dispersion measurements with aqueous solutions of hemoglobin and myoglobin have been performed in the frequency range from 100 kcps to 15 Mcps. The influence of preparation, particle size, and solvent conditions was s

Dielectric properties of hemoglobin and
✍ Peter Schlecht πŸ“‚ Article πŸ“… 1969 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 489 KB

This paper is concerned with the molecular origin of the dipole moment of sperm whale myoglobin as it can be calculated from the dielectric dispersion at 1 Mcps on the basis of a mechanism of orientational polarization. It was possible to compare the dielectric increment of native myoglobin and its