Where children play

Medgyesi, Danielle Nicolle

doi:10.17077/etd.i5nvoexv

Cited by 3 publications

(3 citation statements)

References 54 publications

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“…The existence of at least one murine IgM macroglobulin showing Slaph A binding is compatible with similar observations of human [3,8] and rat [9] IgM proteins and indicates that whatever the mechanism involved, it may be common throughout at least mammalian immunoglobulin evolution.…”

Section: Discussionsupporting

confidence: 83%

The Binding of Murine IgM to Staphylococcal A Protein

1978

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The binding of Staph A protein to murine immunoglobulins has previously been thought to be restricted to the IgG2 and IgG3 classes. In this study five IgM proteins were assessed for binding, and of these one showed marked Staph A binding. Pepsin digestion of this IgM molecule produced several different sized fragments, and the binding studies with these fragments indicated that the binding site is in the CH2 domain.

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Section: Discussionsupporting

confidence: 83%

The Binding of Murine IgM to Staphylococcal A Protein

1978

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“…whereas IgM was not detected in the bound fraction [12]. Recently Medgyesi et al [15] reported that ihe IgGl and lgG2c subclasses of rat IgG interact with protein A, whereas the subclasses IgG2a and IgG2b do noi. Furthermore, these authors also reported that a minor portion (15%) of IgM in normal rat serum binds to protein A as well.…”

Section: Discussionmentioning

confidence: 96%

Determination of the Immunoglobulin Class of Complement‐dependent Cytotoxic Antibodies in Serum of D23 Hepatoma‐bearing Rats

et al. 1980

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The immunoglobulin class of the complement-dependent cytotoxic antibodies in serum from D23 hepatoma-bearing rats (D23 TBS) for D23 hepatoma cells was analysed. When studied by affinity chromatography with concanavalin A, protamine, or staphylococcal protein A conjugated to Sepharose, the cytotoxic activity bound to the former two but not protein A. The binding fractions were further characterized by column chromatography on Sepharose CL-4B. The cytotoxic activity was recovered exclusively in the high molecular weight fractions corresponding to human IgM. Monitoring with IgG- or IgM-specific rabbit antibodies indicated that these high molecular weight cytotoxic fractions contained both IgG and IgM. However, fractionation of D23 TBS at low pH suggested that cytotoxicity was due to IgM antibodies rather than to immune-complexed IgG antibodies. This was supported by the findings that rabbit antirat IgM antibodies inhibited the cytotoxicity of TBS completely when added at high dilutions.

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“…Some variants of IgA [6. 7, 14, 18] and IgM [4,5,7,II,12,14] can also bind to SPA. hi the mouse, it was first reported that myeloma proteins of the IgG!…”

mentioning

confidence: 99%

Interactions between Mouse Immunoglobulins and Staphylococcal Protein A

1979

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When mouse serum or ascites is applied on protein A-Sepharose columns and washed with enough phosphate-buffered saline, a second protein peak is often eluted with the same buffer after the first major peak of unbound proteins. This second peak is almost pure Ig G1. More IgG1 plus IgG2a, IgG2b and IgG3 are thereafter eluted with acid saline. 90% of the IgG1 whichhad been eluted with neutral buffer could be re-eluted at the same retarded position with the same buffer. When a gradient from 0 to 3 M sodium thiocyanate was started after the major peak of unbound proteins, all IgG1 was eluted before IgG2 and IgG3. These results suggest that IgG1 has a much lower affinity for protein A than IgG2 or IgG3 and that normal mouse serum IgG1 can be purified by such a simple procedure.

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Where children play

Abstract: Special thanks to the Terre des hommes leadership team for their hospitality and diligent support for the project;

Cited by 3 publications

References 54 publications

The Binding of Murine IgM to Staphylococcal A Protein

The Binding of Murine IgM to Staphylococcal A Protein

Determination of the Immunoglobulin Class of Complement‐dependent Cytotoxic Antibodies in Serum of D23 Hepatoma‐bearing Rats

Interactions between Mouse Immunoglobulins and Staphylococcal Protein A

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