Interactions of pig Fab mu and Fab alpha fragments with protein A from Staphylococcus aureus
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
PubMed
6772532
DOI
10.1007/bf02877347
Knihovny.cz E-zdroje
- MeSH
- chromatografie afinitní MeSH
- hořčík farmakologie MeSH
- imunoglobulin A metabolismus MeSH
- imunoglobulin M metabolismus MeSH
- imunoglobuliny - alfa-řetězce MeSH
- imunoglobuliny - Fab fragmenty * MeSH
- imunoglobuliny - mu-řetězce MeSH
- prasata MeSH
- stafylokokový protein A metabolismus MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- hořčík MeSH
- imunoglobulin A MeSH
- imunoglobulin M MeSH
- imunoglobuliny - alfa-řetězce MeSH
- imunoglobuliny - Fab fragmenty * MeSH
- imunoglobuliny - mu-řetězce MeSH
- stafylokokový protein A MeSH
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.
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