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.
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Robertson, D.H.L., Beynon, R.J. & Evershed, R.P. Extraction, characterization, and binding analysis of two pheromonally active ligands associated with major urinary protein of house mouse (Mus musculus). J Chem Ecol 19, 1405–1416 (1993). https://doi.org/10.1007/BF00984885
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DOI: https://doi.org/10.1007/BF00984885