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 M(r) 19k and an isoelectric point of 4.7, whereas the pig protein appears to consist of a single polypeptide chain of M(r) 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.
|Autori interni:||DAL MONTE, MASSIMO|
|Autori:||DAL MONTE M; ANDREINI I.; REVOLTELLA; R.P. PELOSI P.|
|Titolo:||Purification and characterization of two odorant binding proteins from nasal tissue of rabbit and pig|
|Anno del prodotto:||1991|
|Digital Object Identifier (DOI):||10.1016/0305-0491(91)90068-O|
|Appare nelle tipologie:||1.1 Articolo in rivista|