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Amino acid sequence of CAP 2b , an insect cardioacceleratory peptide from the tobacco hawkmoth Manduca sexta
Author(s) -
Graham Huesmann,
Clement C. Cheung,
Poh Kheng Loi,
Terry D. Lee,
Kristine M. Swiderek,
Nathan J. Tublitz
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00929-4
Subject(s) - manduca sexta , manduca , edman degradation , insect , peptide sequence , biochemistry , amino acid , peptide , biology , sphingidae , neuropeptide , protein primary structure , botany , gene , receptor
The primary structure of a novel insect neuropeptide, Cardioacceleratory Peptide 2b (CAP 2b ), from the tobacco hawkmoth Manduca sexta has been established using a combination of mass spectroscopy, Edman degradation microsequencing, amino acid analysis, and biological assays. The sequence of CAP 2b , pyroGlu‐Leu‐Tyr‐Ala‐Phe‐Pro‐Arg‐Val‐amide, has a molecular weight of 974.6 and is blocked at both the amino and car☐yl ends. Examination of several national computer protein data bases failed to reveal other peptides or proteins with any sequence homology to CAP 2b indicating that this is likely to be a novel insect neuropeptide. This peptide may be a general activator of insect viscera since it causes an increase in heart rate in Manduca and in Drosophila , and has also been implicated in the regulation of fluid secretion by the Malphigian tubules of Drosophila .