1. Isolation and characterization of a diuretic peptide common to the house fly and stable fly
- Author
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Oanh Truong, Mark S. Wright, G. Mark Holman, Nicholas F. Totty, F. Clottens, Timothy K. Hayes, Geoffrey M. Coast, A. I. Mallet, Iain Kay, Jum-Sook Chung, and Don L. Bull
- Subjects
endocrine system ,medicine.medical_specialty ,Malpighian tubule system ,animal structures ,Stable fly ,Corticotropin-Releasing Hormone ,Physiology ,Molecular Sequence Data ,Peptide ,Stomoxys ,Malpighian Tubules ,Biochemistry ,Mass Spectrometry ,Cellular and Molecular Neuroscience ,Endocrinology ,Houseflies ,Manduca ,Internal medicine ,Cyclic AMP ,medicine ,Animals ,Amino Acid Sequence ,Diuretics ,chemistry.chemical_classification ,Sequence Homology, Amino Acid ,biology ,Muscidae ,fungi ,Protein primary structure ,biology.organism_classification ,chemistry ,Manduca sexta ,Peptides ,Sequence Analysis ,Musca - Abstract
An identical CRF-related diuretic peptide (Musca-DP) was isolated and characterized from whole-body extracts of the house fly, Musca domestica, and stable fly, Stomoxys calcitrans. The peptide stimulates cyclic AMP production in Manduca sexta Malpighian tubules and increases the rate of fluid secretion by isolated Musca domestica tubules. The 44-residue peptide, with a mol.wt. of 5180, is amidated, and has the primary structure: NKPSLSIVNPLDVLRQRLLLEIARRQMKENTRQVELNRAILKNV-NH2. Musca-DP has a high percentage of sequence identity with other characterized CRF-related insect diuretic peptides.
- Published
- 1994
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