Pigs produce only a single form of CGRP, part of which is processed to N- and C-terminal fragments
Research output: Contribution to journal › Journal article › Research › peer-review
T N Rasmussen, M Bersani, A H Johnsen, Hans Kofod, J J Holst
Using radioimmunoassays with two different antisera, one directed towards the C-terminal and one towards the mid part of porcine and human alpha-CGRP, respectively, we isolated three immunoreactive peptides from acid/ethanol extracts of porcine spinal cord by means of HPLC. By amino acid sequence analysis and mass spectrometry (PDMS), the most abundant peptide was found to be identical to the 37 residue CGRP previously isolated from porcine adrenal glands and spinal cord. The two remaining peptides were identified as pCGRP(18-37) and pCGRP(19-37). Furthermore, the oxidized forms (oxidized Met in position 22) of all three peptides were isolated. We extracted a large amount of tissue and the extractable peptides were purified without discarding side fractions. The purification steps were monitored by immunochemical methods that are highly sensitive for human alpha- and beta-CGRP. Yet we were unable to detect any second full-length form of CGRP. Thus, we conclude that only a single form of full-length CGRP is found in pigs and that this peptide may be cleaved to produce potentially bioactive N- and C-terminal fragments.
|Number of pages||6|
|Publication status||Published - 1994|
- Amino Acid Sequence, Animals, Calcitonin Gene-Related Peptide, Mass Spectrometry, Molecular Sequence Data, Peptide Fragments, Radioimmunoassay, Swine