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Insect Biochem Mol Biol

Title:		Isolation and identification of a pheromonotropic neuropeptide from the brain-suboesophageal ganglion complex of Lymantria dispar: a new member of the PBAN family
Author(s):		Masler EP; Raina AK; Wagner RM; Kochansky JP;
Address:		"Insect Neurobiology and Hormone Laboratory, Plant Sciences Institute, USDA-ARS, Beltsville, MD 20705-2350"
Journal Title:		Insect Biochem Mol Biol
Year:		1994
Volume:		24
Issue:		8
Page Number:		829 - 836
DOI:		10.1016/0965-1748(94)90111-2
ISSN/ISBN:		0965-1748 (Print) 0965-1748 (Linking)
Abstract:		"A pheromonotropic peptide was isolated from brain-suboesophageal ganglion complexes of the adult female gypsy moth, Lymantria dispar, using a 5-step HPLC purification protocol and an in vivo bioassay in Helicoverpa zea. The intact peptide was sequenced by automated Edman degradation. The L. dispar pheromone biosynthesis activating neuropeptide (Lyd-PBAN) is a C-terminally amidated 33-amino acid peptide with a molecular weight of 3881. The peptide was synthesized using Fmoc procedures. Lyd-PBAN has sequence homology with Hez-PBAN (81.8%) and Bom-PBAN-I (66.7%). All three PBANs share the C-terminal hexapeptide sequence, Tyr-Phe-Ser-Pro-Arg-Leu-NH2. In addition, the C-terminal pentapeptide sequences of Pseudaletia pheromonotropin (Pss-PT), Bombyx diapause hormone (Bom-DH), the locustamyotropins (Lom-MT) and leucopyrokinin (Lem-PK) are identical or have a high degree of homology to the C-terminus of PBANs"
Keywords:		"Amino Acid Sequence Animals *Brain Chemistry Chromatography, High Pressure Liquid Esophagus/innervation Female Ganglia, Invertebrate/*chemistry Molecular Sequence Data Moths/*chemistry Neuropeptides/chemistry/*isolation & purification Sequence Homology, A;"
Notes:		"MedlineMasler, E P Raina, A K Wagner, R M Kochansky, J P eng England 1994/09/01 Insect Biochem Mol Biol. 1994 Sep; 24(8):829-36. doi: 10.1016/0965-1748(94)90111-2"