Isolation of Human IgA Utilizing Protein a Affinity Chromatography
- 1 January 1982
- journal article
- research article
- Published by Taylor & Francis in Immunological Communications
- Vol. 11 (4) , 283-290
- https://doi.org/10.3109/08820138209050728
Abstract
Human serum IgA was isolated employing a system of G-200 column chromatography, anion exchange (DE-52) chromatography, and passage over protein A and anti-IgG Sepharose 4B columns. Polyacrylamide gel electrophoresis (PAGE) analysis of the isolated immunoglobulin revealed polypeptides corresponding to alpha and light immunoglobulin chains of IgA which were identified immunochemically as IgA. Ultracentrifugation studies revealed that the isolated immunoglobulin co-migrated with 7S IgG markers. This procedure may serve as an alternative to classical isolation procedures of IgA from human serum.This publication has 15 references indexed in Scilit:
- Comparison of Mechanisms of Interaction between Protein A from Staphylococcus aureus and Human Monoclonal IgG, IgA and IgM in Relation to the Classical Fcγ and the Alternative F(ab')2γ Protein A InteractionsScandinavian Journal of Immunology, 1981
- Isolation of Human and Canine IgM Utilizing Protein a Affinity ChromatographyImmunological Communications, 1981
- IgA contamination of IgG prepared on a protein A columnJournal of Immunological Methods, 1979
- Use of staphylococcal protein A as an immunological reagentJournal of Immunological Methods, 1978
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Definition of staphylococcal protein A reactivity for human immunoglobulin G fragmentsImmunochemistry, 1970
- Phylogenetic Insight into Evolution of Mammalian Fc Fragment of γG Globulin Using Staphylococcal Protein AThe Journal of Immunology, 1970
- Immunochemical quantitation of antigens by single radial immunodiffusionImmunochemistry, 1965