Applications of Bacterial Immunoglobulin-Binding Proteins to the Purification of Immunoglobulins View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1993

AUTHORS

Michael D. P. Boyle , Ervin L. Faulmann , Dennis W. Metzger

ABSTRACT

The specificity of the antibody molecule has proved extremely valuable for many applications in affinity chromatography. For these applications to be effective, it is necessary to be able to isolate antibodies of the desired specificity free from other serum components or nonantibody plasma proteins. The majority of the earlier studies utilized polyclonal antibodies generated in a variety of mammalian species, in particular, rabbits and goats. With the advent of monoclonal antibody technology and the ability to produce large quantities of antibodies of a single specificity, these reagents have found broad applications in affinity purification studies. Monoclonal antibodies have an advantage over polyclonal antibodies in that the majority of antibodies in the preparation are directed against the antigen of interest. By contrast, specific antibodies present in a polyclonal hyperimmune serum represent only 5–10% of the total immunoglobulin present. The ability to separate antibodies, monoclonal and polyclonal, from complex mixtures of other plasma proteins or tissue culture fluids is extremely important in obtaining pure sources of antibody for immobilization and use in affinity chromatography. More... »

PAGES

91-112

Book

TITLE

Molecular Interactions in Bioseparations

ISBN

978-1-4899-1874-1
978-1-4899-1872-7

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4899-1872-7_6

DOI

http://dx.doi.org/10.1007/978-1-4899-1872-7_6

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1015421494


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