35Cl nuclear magnetic resonance studies of metal binding to bovine serum albumin
β Scribed by James L. Sudmeier; Joseph J. Pesek
- Publisher
- Elsevier Science
- Year
- 1971
- Tongue
- English
- Weight
- 721 KB
- Volume
- 41
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract The interaction of Ce^3+^ to bovine serum albumin (BSA) has been investigated mainly by fluorescence spectra, UVβvis absorption spectra, and circular dichroism (CD) under simulative physiological conditions. Fluorescence data revealed that the quenching mechanism of BSA by Ce^3+^ was a
Pol~v(dimethyldiul1ylammonii~m chloride) (PDMDAAC) exhibits u strong electrmtatic interaction with bovine serum albumin (BSA) at pH 8.0 in 0.16M NaCl. Electrophoretic. dynamic, und static light scuttering suggest that the mode of binding of BSA to PDMDAAC depends upon the weight concentration ratio