| Literature DB >> 1764106 |
M B Blackburn1, T G Kingan, W Bodnar, J Shabanowitz, D F Hunt, T Kempe, R M Wagner, A K Raina, M E Schnee, M C Ma.
Abstract
A 30-amino acid diuretic peptide was isolated from the corpora cardiaca-corpora allata complexes and, separately, from medial neurosecretory cells of the Sphingid moth, Manduca sexta. The peptide was found to have the following sequence, determined by automated Edman degradation and mass spectrometry: SFSVNPAVDILQHRYMEKV AQNNRNFLNRV-NH2. We have named the peptide Mas-DP II. The peptide was synthesized and shown to possess diuretic activity in decapitated moths. Mas-DP II is related by sequence homology to a 41-amino acid diuretic peptide identified previously from M. sexta, and it belongs to the family of corticotropin releasing factor-like peptides.Entities:
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Year: 1991 PMID: 1764106 DOI: 10.1016/0006-291x(91)92025-f
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575