Title: The propeptide of preprosomatostatin mediates intracellular transport and secretion of alpha-globin from mammalian cells Document date: 1989_5_1
ID: kjid2e3q_31
Snippet: ence of a 142-amino acid foreign protein at the carboxyl terminus of the propeptide, the chimera was recognized by the processing enzymes nearly as efficiently as native proSRIF (70%) and cleaved at the native processing site. The data also indicated that a low percentage of PRO-GLO molecules were cleaved at a single arginine located in the linker region between proSRIF and ot-globin (Fig. 1) . It is possible that we may have generated a cryptic .....
Document: ence of a 142-amino acid foreign protein at the carboxyl terminus of the propeptide, the chimera was recognized by the processing enzymes nearly as efficiently as native proSRIF (70%) and cleaved at the native processing site. The data also indicated that a low percentage of PRO-GLO molecules were cleaved at a single arginine located in the linker region between proSRIF and ot-globin (Fig. 1) . It is possible that we may have generated a cryptic cleavage site in PRO-GLO for a distinct monobasic-processing enzyme thought to be present in secretory granules (38) . In ~1/3 of precursors cleaved at single basic residues, proline immediately precedes or follows the basic amino acid. Consistent with this hypothesis, ProArg was present in the PRO-GLO linker peptide.
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