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Primary structure of a cardioactive neuropeptide from the tobacco hawkmoth, Manduca sexta
Author(s) -
Cheung Clement C.,
Loi Poh Kheng,
Sylwester Andy W.,
Lee Terry D.,
Tublitz Nathan J.
Publication year - 1992
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(92)81436-p
Subject(s) - manduca sexta , peptide , sphingidae , edman degradation , protein primary structure , biochemistry , peptide sequence , manduca , amino acid , biology , chemistry , insect , botany , gene
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‐NH 2 , is identical to a peptide recently isolated from crabs called crustacean cardioactive peptide (CCAP) and we propose that this peptide be named Manduca CCAP.