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 |