| First Author | Pes D | Year | 1995 |
| Journal | Comp Biochem Physiol B Biochem Mol Biol | Volume | 112 |
| Issue | 3 | Pages | 471-9 |
| PubMed ID | 8529023 | Mgi Jnum | J:30486 |
| Mgi Id | MGI:77996 | Doi | 10.1016/0305-0491(95)00063-1 |
| Citation | Pes D, et al. (1995) Odorant-binding proteins of the mouse. Comp Biochem Physiol B Biochem Mol Biol 112(3):471-9 |
| abstractText | After the isolation of two odorant-binding proteins (OBP-I and OBP-II) from mouse nasal tissue, we have purified two additional OBPs, which bind tritiated 2-isobutyl-3-methoxypyrazine. OBP-III is a homodimer with subunits of M(r) 22,000 and pI 4.2. OBP-IV is a homodimer with subunits of M(r) 21,000 and pI 4.85. N-terminal amino acid sequences indicate that OBP-III is identical in its first 40 amino acids to the mouse urinary protein, MUP-5, (ii) OBP-IV is > 90% identical in its first 30 amino acids to the MUP-4, OBP-II is nearly 80% similar in its first 40 amino acids to OBP-I of the rat, and both subunits of OBP-I are > 50% identical with hamster aphrodisin. |
