title: Extraction, characterization, and binding analysis of two pheromonally active ligands associated with major urinary protein of house mouse (Mus musculus).
abstract: Mouse urine contains substantial quantities of a family of proteins (MUPs) that are members of the lipocalycin family of proteins and that are potentially capable of binding hydrophobic molecules. We have used gas chromatography-mass spectrometry (GC-MS) to characterize two ligands associated with the MUPs, a thiazole and a brevicomin derivative. Previous work has suggested a role for these two ligands as androgen-dependent pheromones. In urine, nearly all of these ligands are protein bound and fractionation of MUPs on Mono-Q anion exchange chromatography indicated some specificity of ligand binding by the MUP subclasses.
authors.affiliation: Proteolysis Research Group Department of Biochemistry, The University of Liverpool, P.O. Box 147, L69 3BX, Liverpool, UK.
authors.forename: D H
authors.initials: DH
authors.lastname: Robertson
authors.forename: R J
authors.initials: RJ
authors.lastname: Beynon
authors.forename: R P
authors.initials: RP
authors.lastname: Evershed