Odorant-binding proteins of the mouse

Comp Biochem Physiol B Biochem Mol Biol. 1995 Nov;112(3):471-9. doi: 10.1016/0305-0491(95)00063-1.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cricetinae
  • Electrophoresis, Polyacrylamide Gel
  • Macromolecular Substances
  • Mice
  • Molecular Weight
  • Olfactory Mucosa / chemistry
  • Pyrazines / metabolism
  • Rats
  • Receptors, Odorant / chemistry
  • Receptors, Odorant / isolation & purification*
  • Receptors, Odorant / metabolism
  • Sequence Homology
  • Tritium

Substances

  • Macromolecular Substances
  • Pyrazines
  • Receptors, Odorant
  • odorant-binding protein
  • Tritium
  • 2-isobutyl-3-methoxypyrazine