title: Isolation of two odorant-binding proteins from mouse nasal tissue.
abstract: 1. Two soluble proteins, with good affinity to tritiated 2-isobutyl-3-methoxypyrazine, have been purified from mouse nasal mucosa. 2. The first protein is a heterodimer with subunits of apparent M(r) 18 and 19 kDa and isoelectric point of 4.9; the second is a monomer of M(r) 21 kDa and isoelectric point of 4.8. 3. The characteristics of these binding proteins are compared with those of the other known OBPs and urinary proteins and their putative role is discussed.
authors: Istituto di Industrie Agrarie, Università degli Studi, Pisa, Italy.
authors: D
authors: D
authors: Pes
authors: M
authors: M
authors: Dal Monte
authors: M
authors: M
authors: Ganni
authors: P
authors: P
authors: Pelosi
mesh_terms: D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D051379:Mice; D008970:Molecular Weight; D009297:Nasal Mucosa / Q000737:chemistry*; D011485:Protein Binding; D018035:Receptors, Odorant
chemical_list: D002352:Carrier Proteins; D018035:Receptors, Odorant; C045648:odorant-binding protein