Antigen Binding Properties of Purified Immunoglobulin A and Reconstituted Secretory Immunoglobulin A Antibodies
نویسندگان
چکیده
منابع مشابه
Anticardiolipin Antibodies and Immunoglobulin M and A in Graves’ Disease
Background: Graves’ disease is an autoimmune disease, characterized by the presence of antibodies directed to TSH receptor or nearby regions as well as antibodies to double strands DNA (dsDNA) anticardiolipin and nuclear antibodies. This study evaluated anticardiolipin and rheumatoid factor, such as IgA and IgM antibodies in patients with Graves’ disease. Patients and methods: Anticardiolipin a...
متن کاملInfluence of secretory immunoglobulin A and purified secretory component on dextran-sucrase activity of Streptococcus mutans.
The net stimulation of dextransucrase EC 2.4.1.5) activity from Streptococcus mutans HS6 by dextran, secretory immunoglobulin A, or secretory component was investigated. Approximately equal stimulation resulted from treatment with these three components.
متن کاملDetermination of Superficial Clefts on Fragment of Antigen Binding in Human Immunoglobulin G by Computational Immunology
Background: Immunoglobulins (Igs) are protective glycoproteins specifically identify and eradicate microbes. Fragment of antigen binding (Fab) is a portion of antibody which binds to antigen and consists of one variable and one constant domain of one heavy and one light chain. Idiotypes, epitopes situated on Igs variable region, could be exploited to monitor and target malignant B cells and are...
متن کاملBinding of salivary glycoprotein-secretory immunoglobulin A complex to the surface protein antigen of Streptococcus mutans.
The interaction between a surface protein antigen (PAc) of Streptococcus mutans and human salivary agglutinin was analyzed with a surface plasmon resonance biosensor. The major component sugars of the salivary agglutinin were galactose, fucose, mannose, N-acetylglucosamine, N-acetylgalactosamine, and N-acetylneuraminic acid. Binding of salivary agglutinin to PAc was calcium dependent and heat l...
متن کاملSpecific secondary biological properties of purified rabbit immunoglobulin M and immunoglobulin G antibodies to Brucella abortus and Bordetella pertussis.
Rabbit immunoglobulin (Ig)M and IgG antibodies to Brucella abortus and Bordetella pertussis were isolated as purified products and their specific secondary biological activities were compared. IgM antibodies were found to be more active than IgG proteins in inducing agglutination and sensitization of B. abortus for the complement-dependent bactericidal effect and in inhibiting B. pertussis-indu...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.27.16300