Purification and characterization of two odorant-binding proteins from nasal tissue of rabbit and pig.
1. Soluble proteins showing binding activity to 2-isobutyl-3-methoxypyrazine have been purified to homogeneity from rabbit and pig nasal tissue; their characteristics are similar to the bovine odorant-binding protein and are to be considered members of the same family. 2. The rabbit protein is a homodimer with subunits of Mr 19k and an isoelectric point of 4.7, whereas the pig protein appears to consist of a single polypeptide chain of Mr 22k and an isoelectric point of 4.2. 3. Both proteins bind 2-isobutyl-3-methoxypyrazine with dissociation constants in the micromolar range. 4. Antibodies against the bovine OBP react well with the rabbit protein, and slightly with the porcine one.
Dal Monte
M
M
Istituto di Industrie Agrarie della Università degli Studi, Pisa, Italy.
Andreini
I
I
Revoltella
R
R
Pelosi
P
P
D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002417:Cattle; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007525:Isoelectric Focusing; D007700:Kinetics; D008970:Molecular Weight; D009297:Nasal Mucosa / Q000502:physiology*; D009812:Odorants; D011719:Pyrazines / Q000378:metabolism; D011817:Rabbits; D018035:Receptors, Odorant; D013552:Swine
D002352:Carrier Proteins; D011719:Pyrazines; D018035:Receptors, Odorant; C045648:odorant-binding protein; C034376:2-isobutyl-3-methoxypyrazine