猪源Fab μ片段和Fab α片段与金黄色葡萄球菌蛋白A的相互作用
Interactions of pig Fab mu and Fab alpha fragments with protein A from Staphylococcus aureus.
作者信息
Zikán J
出版信息
Folia Microbiol (Praha). 1980;25(3):254-8. doi: 10.1007/BF02877347.
PMID:6772532
Abstract
Forty % of serum IgM and 47% of dimeric colostral IgA were bound to protein A-Sepharose. Fab mu and Fab alpha fragments showed a reactivity similar to that of the whole immunoglobulins. Complete elutions of IgM and IgA from the protein A-Sepharose were obtained in lower cocentrations of MgCl2 than the complete elution of IgG. However, IgM and IgA were completely eluted at higher concentrations of MgCl2 in the presence of IgG than in its absence.
摘要
40%的血清IgM和47%的二聚体初乳IgA与蛋白A-琼脂糖结合。Fab μ和Fab α片段表现出与完整免疫球蛋白相似的反应性。从蛋白A-琼脂糖上完全洗脱IgM和IgA所需的MgCl2浓度低于完全洗脱IgG所需的浓度。然而，在有IgG存在时，与无IgG时相比，在更高浓度的MgCl2下，IgM和IgA能被完全洗脱。
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