Production and purification of monoclonal IgA antibodies

Tesla, Blanka (2014) Production and purification of monoclonal IgA antibodies. Diploma thesis, Faculty of Science > Department of Biology.

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Abstract

We are constantly exposed to various antigens, most commonly to microorganisms. Antibodies can interact with antigens in different ways and neutralize them. They are produced by B lymphocytes and spread throughout the organism by circulatory, lymphatic and secretory systems. There are five antibody classes, known as IgG, IgA, IgM, IgD and IgE. IgA is the most abundant antibody in mucosal secretion and has an important role against viruses and bacteria. Monoclonal antibodies are typically made by fusing B lymphocytes immunized with desired antigen and myeloma cell line. Monoclonal antibodies are widely used in science and medical practice. The aim of study is to define the best purification method for monoclonal IgA antibodies. The most commonly used method for antibody purification is chromatography. Since there is no well-established protocol for IgA purification, three different chromatography methods were tested: Protein L affinity chromatography, BAKERBOND ABx ion exchanged chromatography and affinity chromatography with peptide used for immunization (Bgl2- a7/8). Purification with Protein L and BAKERBOND ABx were successful, while peptide chromatography was not. Both of these two successful methods have advantages and disadvantages. According to this study, the best method for IgA monoclonal antibody purification was Protein L chromatography.

Item Type: Thesis (Diploma thesis)
Keywords: secretory immunoglobulin, hybridomas, chromatography, ELISA, Campylobacter jejuni, Candida albicans
Supervisor: Oršolić, Nada
Date: 2014
Number of Pages: 48
Subjects: NATURAL SCIENCES > Biology
Divisions: Faculty of Science > Department of Biology
Depositing User: Silvana Šehić
Date Deposited: 12 Nov 2014 09:55
Last Modified: 12 Nov 2014 09:55
URI: http://digre.pmf.unizg.hr/id/eprint/3232

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