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Purification and quantification of heavy‐chain antibodies from the milk of bactrian camels
Author(s) -
Yao Hongqiang,
Zhang Min,
Li Yi,
Yao Jirimutu,
Meng He,
Yu Siriguleng
Publication year - 2017
Publication title -
animal science journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.606
H-Index - 38
eISSN - 1740-0929
pISSN - 1344-3941
DOI - 10.1111/asj.12772
Subject(s) - antibody , immunoglobulin light chain , polyacrylamide gel electrophoresis , gel electrophoresis , affinity chromatography , immunoglobulin g , chemistry , biology , bicinchoninic acid assay , biochemistry , chromatography , microbiology and biotechnology , immunology , enzyme
Camel milk has a unique composition with naturally occurring heavy‐chain antibodies (HCAbs), which exert rehabilitating potencies in infection and immunity. To characterize HCAb in camel milk, immunoglobulin G (IgG) was isolated from the milk of Camelus bactrianus by a combination of affinity chromatography and sodium dodecyl sulfate polyacrylamide gel electrophoresis to purify and size‐fractionate protein A and protein G, which were further identified by Western blotting, and were quantified by bicinchoninic acid (BCA) and ELISA. The results indicated that IgG 1 fraction contains molecules of 50 kDa heavy chains and 36 kDa light chains. The HCAbs (IgG 2 and IgG 3 fractions) devoid of light chains, contain heavy chains of 45 kDa and 43 kDa, respectively, the amounts of which were significantly higher than that of the IgG 1 in the milk of bactrian camels. Above all, we revealed the considerable amounts of HCAbs in the milk of bactrian camels, and developed a novel method for their purification and quantification. These findings provide the basis for developing potential effects of camel milk and its interface with the dairy industry, as well as future investigations of HCAb and its roles in human health and diseases.