Purification and Structural Characterization of Serum Albumin in Bactrian Camel Milk

In this study, the camel serum albumin (CSA) of bactrian camel milk were isolated and purified by DEAE-FF chromatography and Sephacryl S-100 gel filtration, and then amino acid sequence, absolute molecular weight, isoelectric point, amino acid composition and secondary structure of CSA were investigated. The results showed that the purity of CSA was greater than 95% after two steps of purification. Compared with the Camelus ferus SA sequence from the NCBI database (NCBI:XP_006188754), the sequence coverage of CSA was 89%. Its isoelectric point was 4.48 by IEF and the relative molecular mass was 66490.17 Da. CSA contained a full range of amino acid, and essential amino acids accounted for 47.36% of the total amino acids. The most abundant amino acid was glutamic acid, accounting for 12.41% of the total amino acids. The model of total essential amino acids was close to the human body essential amino acid requirements, and CSA was considered to a kind of valuable animal protein resource.High alpha helix content, low beta fold and irregular curl were the main structural characteristics of the CSA.