Characterisation of the main molecular forms of human fecal immunoglobulin A

Clinica Chimica Acta; International Journal of Clinical Chemistry
N KapelD Raichvarg

Abstract

The molecular composition of fecal IgA is poorly documented, although it is of theoretical and practical importance to determine the different forms of IgA in faeces. Two main molecular forms were isolated by successive steps of ion-exchange chromatography and gel-filtration. The first consisted of secretory IgA dimers dissociating into slightly lower molecular mass forms under the influence of the electric field during electrophoresis. The other contained cleaved-IgA complexed with alpha 1-antitrypsin, that is considered to be a serum origin marker. These results confirm that secretory IgA are relatively resistant to digestive enzymes in vivo, and suggest that alpha 1-antitrypsin-bound fragments originate from serum IgA monomers. Analysis of the proportions of these forms may be of value in the investigation of gut diseases.

References

Jan 1, 1977·Preparative Biochemistry·H Khayam-BashiC L Schwartz
Jun 26, 1975·Nature·C R StokesM W Turner
Jan 1, 1986·Annual Review of Immunology·B J Underdown, J M Schiff
Jan 1, 1960·Proceedings of the Society for Experimental Biology and Medicine·H B LEVY, H A SOBER
May 1, 1981·Immunology Today·J Gillon

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Citations

Feb 28, 1993·Clinica Chimica Acta; International Journal of Clinical Chemistry·D MeilletJ G Gobert
May 1, 1993·Transactions of the Royal Society of Tropical Medicine and Hygiene·N KapelJ G Gobert
Jan 1, 1994·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·K R ChintalacharuvuC S Kaetzel

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