Purification, Characterization, and Analysis of the Allergenic Properties of Myosin Light Chain in Procambarus clarkii
Myosin light chain (MLC) plays a vital role in cell and muscle functions and has been identified as an allergen in shrimp.In this study, MLC with a molecular mass of 18 kDa waspurified from crayfish (Procambarus clarkii)muscle.Its physicochemical characterization showed that the purified MLC is a glycoprotein with 4.3% caroohydrate,highly stable to hest,acid-alkali, and digestion, and weakly retains IgE-blinding activity when its secondary structure was altered.serological assays(sugggested that conformational epitopes predominate over linear epitopes in the purified MLC.Two isoforms of the MLC gene(MLC1 and MLC2) were cloned, and the purified MLC was identified as MLC1.Analysis of the secondary and tertaiary structures ofthe MLCs indicated that MLC1 has four conformational epitopes and three linear epitopes,whereas MLC2 had a major conformational epitope and three linear epitopes.These results for understanding hypersensitization of humans to crayfish.
procambarus clarkii myosin light chain purification physicochemical characterization allergenicity epitopes
Yong-Xia Zhang Heng-Li Chen Soheila J.Maleki Min-Jie Cao Ling-Jing Zhang Wen-Jin Su Guang-Ming Liu
College of Food and Biological Engineering,Fujian Collaborative Innovation Center for Exploitation a Agriculture Research Service, Southern Regional Research Center, U.S.Department of Agriculture, 1100
国内会议
2015年福建省水产学会学术年会暨省科协第十五届学术年会卫星会议
福州
英文
309-320
2015-09-01（万方平台首次上网日期，不代表论文的发表时间）