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.

Purification and characterization of two odorant binding proteins from nasal tissue of rabbit and pig

DAL MONTE, MASSIMO;PELOSI, PAOLO
1991

Abstract

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.
DAL MONTE, Massimo; Andreini, I.; Revoltella, ; Pelosi, Paolo
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11568/205116
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