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 |
|---|---|
| Pages (from-to) | 5463-5466 |
| Number of pages | 4 |
| Journal | Journal of Biological Chemistry |
| Volume | 258 |
| Issue number | 9 |
| State | Published - Jan 1 1983 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Purification and amino acid sequence of a noncalcitonin secretory peptide derived from preprocalcitonin. / Birnbaum, R. S.; Mahoney, W.; Roos, B. A.
In: Journal of Biological Chemistry, Vol. 258, No. 9, 01.01.1983, p. 5463-5466.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Purification and amino acid sequence of a noncalcitonin secretory peptide derived from preprocalcitonin
AU - Birnbaum, R. S.
AU - Mahoney, W.
AU - Roos, B. A.
PY - 1983/1/1
Y1 - 1983/1/1
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0020541133&partnerID=8YFLogxK
M3 - Article
C2 - 6853528
AN - SCOPUS:0020541133
VL - 258
SP - 5463
EP - 5466
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 9
ER -