Interactions of pig Fab gamma fragments with protein A from Staphylococcus aureus
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
PubMed
6772531
DOI
10.1007/bf02877346
Knihovny.cz E-zdroje
- MeSH
- chromatografie afinitní MeSH
- dinitrofenoly imunologie MeSH
- hořčík farmakologie MeSH
- imunoglobulin G metabolismus MeSH
- imunoglobuliny - Fab fragmenty * MeSH
- imunoglobuliny - Fc fragmenty MeSH
- králíci MeSH
- lehké řetězce imunoglobulinů MeSH
- lidé MeSH
- prasata MeSH
- sefarosa MeSH
- sérový albumin imunologie MeSH
- skot MeSH
- stafylokokový protein A metabolismus MeSH
- těžké řetězce imunoglobulinů MeSH
- zvířata MeSH
- Check Tag
- králíci MeSH
- lidé MeSH
- skot MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- dinitrofenoly MeSH
- hořčík MeSH
- imunoglobulin G MeSH
- imunoglobuliny - Fab fragmenty * MeSH
- imunoglobuliny - Fc fragmenty MeSH
- lehké řetězce imunoglobulinů MeSH
- sefarosa MeSH
- sérový albumin MeSH
- stafylokokový protein A MeSH
- těžké řetězce imunoglobulinů MeSH
Ninety % of pig serum IgG was bound to protein A-Sepharose. Both individual fractions of the IgG, separated on the basis of their electric charge, were adsorbed on protein A-Sepharose to a similar extent. However, these fractions differed in their elution profile from the protein A-Sepharose when a gradient of increasing molarity of MgCl2 was used. Relative amounts of fractions eluted in higher concentrations of MgCl2 were augmented with the increasing amount of IgG bound to SpA-Sepharose. Not only high proportions of Fc fragments, but also nearly half of Fab fragments reacted with protein A. This latter interaction, confirmed also by affinity electrophoresis, did not have the character of a specific reaction of antibody with antigen.
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