Abstract
A previous report from this laboratory provided immunochemical and biochemical evidence for the existence of a secretory peptide derived from the noncalcitonin region of rat preprocalcitonin. By a variety of criteria, we demonstrated that this naturally occurring peptide was similar, if not identical, to a synthetic peptide which consisted of the NH2-terminal 16 residues of the calcitonin mRNA translation product. We have now purified this peptide from rat medullary thyroid carcinoma and sequenced it. A rat tumor of the 1-2-4 tumor series was extracted in 0.1 N HCl yielding 900 μg of immunoreactive peptide. The peptide was purified to homogeneity by: trichloroacetic acid precipitation of contaminating protein; gel filtration; and finally, reverse phase high pressure liquid chromatography. Overall yield was approximately 24%. Amino acid analysis and sequencing of the peptide yielded a composition and sequence identical with that of the synthetic peptide.
Original language | English (US) |
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Pages (from-to) | 5463-5466 |
Number of pages | 4 |
Journal | Journal of Biological Chemistry |
Volume | 258 |
Issue number | 9 |
State | Published - 1983 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology