Abstract
The amino acid sequence of the first of a family of insect cardioregulatory peptides from the tobacco hawkmoth, Manduca sexta, has been determined using a combination of Edman degradation microsequencing and mass spectroscopy. This peptide contains 9 amino acid residues and an observed mass for the monoisotopic protonated molecule of 956.4 Da. There are two cysteines at positions 3 and 9 forming a disulfide bridge and the carboxyl-terminus is amidated. The structure of this peptide, Pro-Phe-Cys-Asn-Ala-Phe-Thr-Gly-Cys-NH2, is identical to a peptide recently isolated from crabs called crustacean cardioactive peptide (CCAP) and we propose that this peptide be named Manduca CCAP.
Original language | English (US) |
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Pages (from-to) | 165-168 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 313 |
Issue number | 2 |
DOIs | |
State | Published - Nov 23 1992 |
Externally published | Yes |
Keywords
- Cardioregulation
- Insect neuropeptide
- Invertebrate neuropeptide
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology