Sulfation is a common post-translational modification of tyrosine residues in eukaryotes, but has not been observed in yeast and prokaryotes. Sulfation is limited to secretory and transmembrane proteins that have passed the trans-Golgi network, where two membrane-bound tyrosylprotein sulfotransferase enzymes catalyze the transfer of sulfate from adenosine 3’-phosphate 5’-phosphosulfate to the tyrosine phenol. Lit.
|
λ / nm |
ε / M-1 cm-1 |
|---|---|
| 214 | 0 |
| 240 | 0 |
| 245 | 0 |
| 250 | 0 |
| 255 | 0 |
| 260 | 0 |
| 265 | 0 |
| 270 | 0 |
| 272 | 0 |
| 274 | 0 |
| 276 | 0 |
| 278 | 0 |
| 280 | 0 |
| 282 | 0 |
| 284 | 0 |
| 286 | 0 |
| 288 | 0 |
| 290 | 0 |
| 292 | 0 |
| 294 | 0 |
| 296 | 0 |
| 298 | 0 |
| 300 | 0 |
| 302 | 0 |
| 304 | 0 |
| 306 | 0 |
| 308 | 0 |
| 310 | 0 |
| 312 | 0 |
| 314 | 0 |
| 316 | 0 |
| 318 | 0 |
| 320 | 0 |