Primary structure of a cardioactive neuropeptide from the tobacco hawkmoth, Manduca sexta.
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.
Cheung
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Institute of Neuroscience, University of Oregon, Eugene 97403.
Loi
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Sylwester
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Lee
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Tublitz
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D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D007301:Insect Hormones / Q000737:chemistry*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009036:Moths / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry*; D011761:Pyrrolidonecarboxylic Acid / Q000031:analogs & derivatives
D007301:Insect Hormones; D009842:Oligopeptides; C044833:adipokinetic hormone; D011761:Pyrrolidonecarboxylic Acid