@article {3480,
	title = {The SepOvotropin: a new ovarian peptide regulating oocyte transport in Sepia officinalis.},
	journal = {Biochem Biophys Res Commun},
	volume = {276},
	year = {2000},
	month = {2000 Oct 5},
	pages = {1013-8},
	abstract = {<p>In the cuttlefish Sepia officinalis, the successive steps of egg laying are controlled by multiple neuropeptides. Recent experiments led us to suppose that there was possible involvement of a second regulation pathway by the release of ovarian regulatory peptides in the genital tract. Using HPLC fractionation and an in vitro biological test, a C-terminal amidated peptide modulating the motility of the Sepia officinalis oviduct was isolated from an extract of vitellogenic ovarian follicles. The mass of this peptide as determined by MALDI-TOF (1501.8 Da) and analysis by Edman degradation led to the following sequence: Pro-Lys-Asp-Ser-Met-Leu-Leu-Leu-Gln-Val-Pro-Val-Tyr-amide. The peptide mapping performed by LC/MS revealed a distribution restricted to the follicles, the full grown oocytes and the eggs. This new peptide, called SepOvotropin, modulated contractions of the whole genital tract in physiological conditions from a threshold concentration between 10(-20) and 10(-19) M, demonstrating for the first time the occurrence of a specific peptidergic control of egg-laying in cephalopods.</p>
},
	keywords = {Amino Acid Sequence, Animals, Chromatography, High Pressure Liquid, Female, Molecular Weight, Mollusca, Muscle Contraction, Oocytes, Ovarian Follicle, Oviducts, Oviposition, Paracrine Communication, Peptide Mapping, Peptides, Pheromones, Seawater, Sensitivity and Specificity, Sequence Analysis, Protein, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization},
	issn = {0006-291X},
	doi = {10.1006/bbrc.2000.3595},
	author = {C{\'e}line Zatylny-Gaudin and Gagnon, Jean and Boucaud-Camou, Eve and Jo{\"e}l Henry}
}
