Identification of Polypeptides Constituting Lactophorin by Monoclonal Antibody to Bovine Milk Lactophorin
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概要
- 論文の詳細を見る
A monoclonal antibody to lactophorin (LP) was prepared by creating hybridoma from mouse myeloma cells and spleen cells from mice immunized with PAS-4 concentrated fraction from bovine milk fat globule membrane. The prepared antibody recognized a polypeptide moiety of LP27, the major component constituting LP, but not a carbohydrate moiety. Immunoblot analysis showed that all polypeptides (LP17, LP20, LP27, LP40, and LP50) constituting LP were recognized by the antibody. The identities of LP20, LP40, and LP50 were verified by N-terminal and internal amino acid sequencing. LP20 contains hydrolysate of LP27 besides LP27 without the O-glycosyl sugar chain. These results suggest that LP40 and LP50 are homo- or heterodimers of LP20 and LP27. This is the first report to the effect that LP was constructed from several forms of polypeptides, derived from LP27.
- 社団法人 日本農芸化学会の論文
著者
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Azuma Norihiro
Department Of Agricultural Chemistry The University Of Tokyo
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Kanno Choemon
Department Of Animal Science Utsunomiya University
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Motoshima Hidemasa
Research Center Yotsuba Milk Products Co. Ltd.
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UENO Tomoya
United Graduate School of Agricultural Science, Tokyo University of Agriculture and Technology
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Motoshima Hidemasa
Research and Development Department, Yotsuba Milk Products Co.
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KANNO Choemon
Department of Applied Biochemistry, College of Agriculture, Utsunomiya University
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