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Competent Antigen-Binding Fragments (Fab) from Secretory Immunoglobulin A Using Streptococcus sanguis Immunoglobulin A Protease

descriptionPublicationkeyboard_double_arrow_right Article 01 Jan 1984Publisher:S. Karger AGJournal:Caries Research, volume 18, pages 201-208 (issn: 0008-6568, eissn: 1421-976X,

Authors: C. P. Mallett; D. L. Everhart; Robert J. Boylan;

doi: 10.1159/000260766

pmid: 6423284

Competent Antigen-Binding Fragments (Fab) from Secretory Immunoglobulin A Using Streptococcus sanguis Immunoglobulin A Protease

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Abstract

Immunoglobulin A (IgA) protease, a family of bacterial enzymes, cleaves human IgA1 at a single bond generating distinct Fab and Fc fragments. Purified secretory IgA with known specificity for Streptococcus mutans NCTC 10449 (serotype c) was hydrolyzed with IgA protease prepared from Streptococcus sanguis ATCC 10556. The isolated Fab fragments retained their initial activity by specifically binding to antigen and by deterring the sucrose-dependent adherence of S. mutans to glass indicating that the antigen-binding fragments behave as immunologically competent elements.

Related Organizations

New York University
United States
University of Chicago
United States

Keywords

Antigens, Bacterial, Immunodiffusion, Serine Endopeptidases, Enzyme-Linked Immunosorbent Assay, Antigen-Antibody Reactions, Streptococcus mutans, Immunoglobulin Fab Fragments, Immunoglobulin A, Secretory, Humans, Streptococcus sanguis, Saliva, Immunoelectrophoresis, Peptide Hydrolases

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	impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.	Average