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FEBS Lett

Title:		"Odorant and pheromone binding by aphrodisin, a hamster aphrodisiac protein"
Author(s):		Briand L; Huet J; Perez V; Lenoir G; Nespoulous C; Boucher Y; Trotier D; Pernollet JC;
Address:		"Biochimie et Structure des Proteines, INRA UR 477, Jouy-en-Josas Cedex, France"
Journal Title:		FEBS Lett
Year:		2000
Volume:		476
Issue:		3
Page Number:		179 - 185
DOI:		10.1016/s0014-5793(00)01719-1
ISSN/ISBN:		0014-5793 (Print) 0014-5793 (Linking)
Abstract:		"Aphrodisin is a soluble glycoprotein of hamster vaginal discharges, which stimulates male copulatory behavior. Natural aphrodisin was purified and its post-translational modifications characterized by MALDI-MS peptide mapping. To evaluate its ability to bind small volatile ligands, the aphrodisiac protein was expressed in the yeast Pichia pastoris as two major isoforms differing in their glycosylation degree, but close in conformation to the natural protein. Dimeric recombinant aphrodisins were equally able to efficiently bind odors (2-isobutyl-3-methoxypyrazine and methyl thiobutyrate) and a pheromone (dimethyl disulfide), suggesting that they could act as pheromone carriers instead of, or in addition to, direct vomeronasal neuron receptor activators"
Keywords:		Animals Cricetinae Female Male Mass Spectrometry Mesocricetus Odorants Pheromones/chemistry/genetics/*metabolism Pichia/genetics Protein Binding Proteins/chemistry/genetics/*metabolism Recombinant Proteins/chemistry/genetics/metabolism Sex Attractants/che;
Notes:		"MedlineBriand, L Huet, J Perez, V Lenoir, G Nespoulous, C Boucher, Y Trotier, D Pernollet, J C eng England 2000/07/29 FEBS Lett. 2000 Jul 7; 476(3):179-85. doi: 10.1016/s0014-5793(00)01719-1"