| Autor: |
Ahmed, Razia H., Nieves, Jaime, Kim, Lisa, Echegoyen, Luis, Puett, David |
| Zdroj: |
Journal of Protein Chemistry; October 1987, Vol. 6 Issue: 5 p431-439, 9p |
| Abstrakt: |
The binding of vanadyl to a porcine and bovine testicular S-100-like protein and to calmodulin was demonstrated using X-band (9.2 gHz) electron paramagnetic resonance (EPR) spectroscopy in aqueous solution at pH 7.4. In liquid solutions at 22°C, the vanadyl-protein complexes yielded VO2+near rigid limit spectra. At 122 K, each of the three high-field resonances (i.e., 3/2, 5/2, and 7/2 parallel components) splits into two components indicating the presence of two classes of vanadyl-binding sites in each protein. The spectra of the frozen solutions were simulated to give parallel and perpendicular components of the hyperfine coupling constant and g factors similar to other vanadyl-protein complexes. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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