A novel method using immuno-affinity chromatography for isolating β-conglycinin from soybean proteins
A monoclonal antibody (Mab) 6G4 against soybean β-conglycinin has been prepared using a conjugate of chicken ovalbumin and a synthetic peptide that corresponded to one of the epitope sequences of β-conglycinin as the immunogen.An ELISA method for the quantification of β-conglycinin has also been developed.In the present study, we report a novel method for the purification of β-conglycinin by Mab 6G4-based immuno-affinity chromatography.β-Conglycinin with a purity of 92.9% was successfully isolated from soybean proteins.Western blot assay was used to further identify its characteristics and the results demonstrated that the purified β-conglycinin maintains its biological activities.Therefore,the Mab-based immuno-affinty chromatography is an available method for purification of β-conglycinin.It also provides a new opportunity for future study on the mechanism of food allergy responses using high purity β-conglycinin as the experimental material.
β-Conglycinin Monoclonal antibody (Mab) Immuno-affinity chromatography Purification
Jinming You Peng Sun Defa Li Shiyan Qiao Mingren Qu Zirui Wang Guanhong Li Ke Pan
College of Animal Science and Technology, Jiangxi Agricultural University, No.1101 Zhimin Road, Nanc National Key Laboratory of Animal Nutrition, China Agricultural University, No.2 West Yuanmingyuan R
国内会议
南昌
英文
182-185
2015-10-01（万方平台首次上网日期，不代表论文的发表时间）