Cloning, Monoclonal Antibody Production, and Bodily Distribution Pattern of a Bovine Lipocalin

A bovine lipocalin, previously identified as a putative odorant-binding protein in bovine colostrum (bcOBP), was cloned and expressed, and its monoclonal antibody was established. bcOBP was constantly secreted into milk on day of parturition until at least 10 d postpartum at a concentration of 181±3...

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Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2012, Vol.76 (4), p.712-720
Main Authors: JAPARIDZE, Tamar, SENDA, Akitsugu, NOZAKI, Hirofumi, YANAGIDA, Mayumi, SUZUKI, Takumi, GANZORIG, Khuukhenbaatar, KUSHI, Yasunori, KIDA, Katsuya, URASHIMA, Tadasu, BRUCKMAIER, Rupert M., FUKUDA, Kenji
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Animals
Antibodies, Monoclonal - biosynthesis
Biological and medical sciences
Body Fluids - chemistry
Cattle - metabolism
Cloning, Molecular
colostrum
Colostrum - chemistry
CxxxC motif
Female
Fundamental and applied biological sciences. Psychology
Lactation - physiology
Lipocalins - chemistry
Lipocalins - genetics
Lipocalins - metabolism
Mice
Mice, Inbred BALB C
Milk - chemistry
Milk Proteins - chemistry
Milk Proteins - genetics
Milk Proteins - metabolism
odorant-binding protein
Organ Specificity
pheromone
Pheromones - metabolism
Pregnancy
Species Specificity
Time Factors
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Summary:A bovine lipocalin, previously identified as a putative odorant-binding protein in bovine colostrum (bcOBP), was cloned and expressed, and its monoclonal antibody was established. bcOBP was constantly secreted into milk on day of parturition until at least 10 d postpartum at a concentration of 181±39 μg/L. Besides milk, bcOBP occurred in the nasal mucus, saliva, amniotic fluid, vaginal discharge, and blood plasma. Despite its low concentration, the distribution pattern and the finding that bcOBP harbored a characteristic sequence motif, CxxxC, which is conserved among insect and mammal pheromone binding proteins, suggest that bcOBP functions as a pheromone carrier. The presence of bcOBP in the plasma at varied concentrations depending on the lactation period does not exclude the possibility that bcOBP is secreted into milk from the blood. Cross-reactivity of the monoclonal antibody indicated presence of proteins homologous to bcOBP in the colostrum of farm animals of Cetartiodactyla.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.110840