Peptides synthesized by a human medullary thyroid carcinoma were purified to homogeneity by reverse-phase high performance liquid chromatography and structurally characterized by determination of amino acid composition, amino add sequence, and fast atom bombardment mass spectra. The katacalcin-related material in the tumor extract was heterogeneous. Katacalcin (1–21) represented the predominant molecular form but metabolites, identified as katacalcin (1–20), (1–19), (1–15) and (1–13), were also identified in high concentration. Calcitonin gene-related peptide-I was isolated from the tumor but caldtonin gene-related peptide-II was absent A minor component of calcitomin gene-related peptide-like immunoreactivity was of higher molecular weight and may represent an incompletely processed form of the prohormone. Gastrin-releasing peptide (1–27) and gastrin-releasing peptide (18–27) (neuromedin C) were isolated from the tumor but gastrin-releasing peptide (14–27) and bom-besin were absent.
|Number of pages||5|
|Publication status||Published - May 1988|
ASJC Scopus subject areas
- Cancer Research