表位
克氏原螯虾
化学
肌球蛋白
生物化学
基因亚型
蛋白质二级结构
分子生物学
小龙虾
生物
抗原
基因
遗传学
渔业
作者
Yongxia Zhang,Heng-Li Chen,Soheila J. Maleki,Min‐Jie Cao,Ling‐Jing Zhang,Wen‐Jin Su,Guangming Liu
标识
DOI:10.1021/acs.jafc.5b01318
摘要
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 was purified from crayfish (Procambarus clarkii) muscle. Its physicochemical characterization showed that the purified MLC is a glycoprotein with 4.3% carbohydrate, highly stable to heat, acid-alkali, and digestion, and weakly retains IgE-binding activity when its secondary structure was altered. Serological assays suggested 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 tertiary structures of the 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 are significant for understanding hypersensitization of humans to crayfish.
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