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J. Dairy Sci. 2009. 92:4992-4996. doi:10.3168/jds.2009-2306
© 2009 American Dairy Science Association ®
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Short communication: Evidence for the presence of a putative odorant-binding protein in bovine colostrum

K. Fukuda*, A. Senda*, T. Ishii{dagger}, T. Urashima*, M. Morita{ddagger} and T. Terabayashi§,1

* Department of Animal and Food Hygiene, and
{dagger} Department of Pathobiological Science, Obihiro University of Agriculture and Veterinary Medicine, 2-11 Inada-cho, Obihiro, Hokkaido 080-8555, Japan
{ddagger} Tokyo Laboratories, Toko Pharmaceutical Industries Co. Ltd., 199-14 Shikahama, Adachi-ku, Tokyo 123-0864, Japan
§ Department of Chemistry, School of Science, Kitasato University, 1-15-1 Kitasato, Sagamihara, Kanagawa 228-8555, Japan

1 Corresponding author: terabaya{at}sci.kitasato-u.ac.jp

Using a combination of PAGE and mass spectrometry for protein identification, we obtained evidence that a putative odorant-binding protein, designated hypothetical protein LOC517854, occurs in bovine colostrum. This protein, termed as a putative bovine colostral odorant-binding protein (bcOBP), consists of 172 AA residues, including a putative 16-AA signal peptide. The theoretical isoelectric point value and molecular mass of the full-length sequence of bcOBP were calculated to be 4.57 and 19604.18, respectively. The highest sequence similarity (83%) was observed with a potential pheromone transporter, Allergen Bos d 2. An odorant-binding protein derived from bovine nasal mucosa showed relatively low sequence similarity (52%) against bcOBP. Its biological function is unclear, but pheromone transport could be considered. This is the first report of a putative odorant-binding protein in bovine colostrum.

Key Words: colostrum • lipocalin • odorant-binding protein • pheromone transport






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