A new prosomatostatin-derived peptide reveals a pattern for prohormone cleavage at monobasic sites.

@article{Benoit1987ANP,
  title={A new prosomatostatin-derived peptide reveals a pattern for prohormone cleavage at monobasic sites.},
  author={Robert Benoit and Nicholas Ling and Frederick Stephen Esch},
  journal={Science},
  year={1987},
  volume={238 4830},
  pages={
          1126-9
        }
}
Cleavage of the peptide bonds of preprosomatostatin at basic residues near the carboxyl terminus yields somatostatin-14, somatostatin-28, and somatostatin-28 (1-12). However, little is known about the molecular forms derived from the amino terminal portion of the precursor, even though this part of the prohormone is highly conserved through evolution. By using an antibody against the amino terminus of prosomatostatin, a decapeptide with the structure Ala-Pro-Ser-Asp-Pro-Arg-Leu-Arg-Gln-Phe… CONTINUE READING

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