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J. Dairy Sci. 89:3400-3407
© American Dairy Science Association, 2006.

Characterization of Bovine Neutrophil Gelatinase-Associated Lipocalin

H. A. van Veen1, M. E. J. Geerts, R. A. A. Zoetemelk, J. H. Nuijens and P. H. C. van Berkel2

Pharming, Archimedesweg 4, 2333 CN Leiden, The Netherlands

1 Corresponding author: h.veen{at}pharming.com

A protein of relative molecular mass of approximately 25,000 was purified from bovine colostrum by cation-exchange and size-exclusion chromatography. The N-terminus of the protein matched the sequence predicted by the National Center for Biotechnology Information for the bovine homolog of human neutrophil gelatinase-associated lipocalin, a glycoprotein of relative molecular mass 25,000 belonging to the family of lipocalins. The protein was further designated as bovine neutrophil gelatinase-associated lipocalin (bNGAL). Sodium dodecyl sulfate-PAGE of enzymically deglycosylated bNGAL indicated that the intact protein bears one N-linked glycan. Monosaccharide and mass spectrometric analyses of released N-linked carbohydrates revealed the presences of complex- and hybrid-type glycans, with galactose substituted with N-acetylgalactosamine. This substitution is typical for glycoproteins expressed in the bovine mammary gland. A specific ELISA revealed bNGAL concentrations in plasma and mature milk of about 0.05 and 1 µg/mL, respectively, whereas values as high as 51 µg/mL were measured in colostrum. Thus, we have isolated and characterized a novel bovine (milk) protein that is a new member of the lipocalin family.

Key Words: neutrophil gelatinase-associated lipocalin • lactoferrin • colostrum






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