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| Content Provider | Springer Nature Link |
|---|---|
| Author | Antimova, O. I. Grudinina, N. A. Egorov, V. V. Polyakov, D. S. Il’in, V. V. Shavlovskii, M. M. |
| Copyright Year | 2016 |
| Abstract | Interaction of the dye Congo red (CR) with fibrils of three model proteins—hen egg lysozyme, recombinant human beta 2-microglobulin (b2M), and recombinant human transthyretin (TTR)—has been investigated using spectrophotometry. Considerable amounts of impurities were detected in the commercial dye formulation. A procedure of dye purification has been developed. The molar extinction coefficient of the dye at 490 nm (ε$_{490}$) has been measured; the coefficient was 3.3 × 10$^{4}$ M$^{–1}$ cm$^{–1}$ at pH > 6.0. The formation of a complex between CR and the fibrils was accompanied by a change in the absorption spectrum of the dye in the visible wavelength range. Titration of fibril solutions with excessive amounts of dye showed that the number of CR molecules bound to a protein monomer within the lysozyme fibrils was close to five, whereas the respective ratio for b2M was close to four, and the ratio for TTR fibrils was close to four molecules per protein subunit. |
| Starting Page | 468 |
| Ending Page | 475 |
| Page Count | 8 |
| File Format | |
| ISSN | 1990519X |
| Journal | Cell and Tissue Biology |
| Volume Number | 10 |
| Issue Number | 6 |
| e-ISSN | 19905203 |
| Language | English |
| Publisher | Pleiades Publishing |
| Publisher Date | 2016-12-15 |
| Publisher Place | Moscow |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | amyloidosis amyloidogenic proteins lysozyme beta2-microglobulin transthyretin Congo red spectrophotometry Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology |
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