## Abstract The interactions between the protein, bovine plasma albumin, and surfactant, sodium dodecyl sulfate, have been studied by ^13^C‐nmr spectroscopy at pH 5.4–6.8 in D~2~O solution. The ^13^C chemical shifts and the ^13^C spin‐lattice relaxation time of the individual carbons of the surfact
Optical property of bovine plasma albumin between 2 and 82 eV
✍ Scribed by T. Inagaki; R. N. Hamm; E. T. Arakawa; R. D. Birkhoff
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1975
- Tongue
- English
- Weight
- 474 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
The optical constants of bovine plasma albumin in the form of a dry solid film have been determined in the 2–82 eV region of photon energy. The extinction coefficient k was obtained by transmission measurements on thin films on a calcium fluoride substrate and on ultrathin films of polystyrene supported by mesh screen. The refractive index n was determined by a Kramers–Kronig analysis using the measured values of k. The complex dielectric function ε and the energy‐loss function −Im(1/ε) for charged particles were derived from the data of n and k. The result for k exhibit, in addition to the well‐known absorptions at 4.4, 5.5, and 6.4 eV, a small peak at 7.6 eV, a shoulder around 9.7 eV, and a strong peak at 14.0 eV. A prominent peak at 22.7 eV in the energy‐loss function exhibits a large degree of collective nature.
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