Spelling suggestions: "subject:"immunoglobulin E""
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A study of the macrophage in the immune responseGroves, David Lynn, January 1967 (has links)
Thesis (Ph. D.)--University of Wisconsin, 1967. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliography.
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A study of influenza in cattle and sheepNakamura, Robert Masayuki, January 1966 (has links)
Thesis (M.S.)--University of Wisconsin--Madison, 1966. / eContent provider-neutral record in process. Description based on print version record. Bibliography: l. 60-65.
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Serum protein absorption by the fetal and new-born guinea pigLeissring, John Cother. January 1961 (has links)
Thesis (M.S.)--University of Wisconsin--Madison, 1961. / Typescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 76-82).
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A study of thyroid-stimulating immunoglobulins in thyroid diseasesTeng, Chong-shing. January 1980 (has links)
Thesis (M.D.)--University of Hong Kong, 1980. / Also available in print.
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Knowledge based structure modeling of the third hypervariable region of antibodies /Galens, Kevin. January 2006 (has links)
Thesis (M.S.)--Rochester Institute of Technology, 2006. / Typescript. Includes bibliographical references (leaves 49-50).
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Characterisation of single domain antibody fragments from the nurse shark Ginglymostoma cirratum, using phage displayDooley, Helen January 2001 (has links)
No description available.
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Production of recombinant human CD21 and CD23 : towards a better understanding of their interactionVan Zyl, Dwain George January 2013 (has links)
The prevalence of allergic diseases has dramatically increased over the last three decades. Presently, it is estimated that 20-30 per cent of the developed world suffers from allergic diseases. The majority of allergic diseases are rooted in the activities of IgE; an immunoglobulin which exerts its effector functions by interacting with a network of proteins. This network includes its low affinity receptor CD23. Cross linking of membrane IgE and CD21 by soluble CD23 results in an increase in IgE synthesis. This marks the interaction between CD23 and CD21 as an attractive therapeutic target. However, details regarding this interaction are inadequate for rational drug design. To obtain a deeper understanding of the CD23-CD21 interaction recombinant human CD21 (SCR1-2 and SCR5-8) and CD23 (16 kD and 25 kDa) were produced. The cloning, expression and purification of recombinant proteins comprised a significant portion of this study. Recombinant CD23 was expressed as inclusion bodies, refolded by rapid dilution and purified by size exclusion chromatography. Conversely, recombinant CD21 was expressed as soluble MBP-fusions and purified with an amylose affinity resin. The interaction between recombinant CD23 and CD21 was analysed by flow cytometry and ELISA experiments. Flow cytometry showed that 16 kDa and 25 kDa CD23 interacted with SCR5-8 to the same extent. Semi-quantitative ELISA experiments showed that both SCR1-2 and SCR5-8 were able to interact with 16 kDa and 25 kDa CD23. This suggests that the binding sites of SCR1-2 and SCR5-8 occur on 16 kDa CD23. Furthermore, since proteins were expressed in E. coli it suggests that the CD23-CD21 interaction does not require glycosylation. Furthermore, considering what is known about the SCR1-2-CD23 interaction from previous NMR studies; i.e. that the C-terminal tail (residues residues 289-298) of CD23 is responsible for binding SCR1-2, indicates that SCR5-8 binds somewhere within the lectin domain of CD23. This indicates that the CD23-CD21 interaction involves C-terminal tail-SCR1-2 and lectin domain-SCR5-8 interactions.
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Separation of immunoglobulins from egg yolk using metal chelate interaction chromatography and ion exchange chromatographyMcCannel, Anne Marie January 1988 (has links)
The immune response of chickens immunized with β-N-acetylglucosaminidase was monitored in the egg yolks of the birds using an enzyme-linked immunosorbent assay. Significantly higher levels of specific antibodies were detected in the yolks of the birds immunized with the enzyme when compared with the yolks of a control bird collected over the same period significant differences also were found in the response within the immunized group of birds, indicating individual variability to the injections.
Immunoglobulins were isolated from egg yolk after a preliminary purification using alginate to precipitate lipoproteins. A ten millilitre DEAE-Sephacel ion exchange chromatography column resulted in a final product containing 16 mg of IgG with a purity of 60% when 50 mL of an egg yolk supernatant was applied. Specific antibody activity toward the antigens β-lactoglobulin and E. coli lipopolysaccharide was higher in both cases in the isolated immunoglobulin fractions which contained lower purity (40%). Lower antibody activity was observed in the 60% purified fractions. Separation of specific antibodies from non-specific antibodies appeared to occur, possibly due to the given characteristics of the specific antibodies, or due to the differences exhibited by chicken IgG subpopulations.
Using metal chelate interaction chromatography, a 10 mL copper-loaded column was able to yield 104 mg of IgG with a purity of 75% when 200 mL egg yolk supernatant was applied. Again, the heterogeneous nature of chicken IgG was illustrated.
A comparison of the two chromatographic techniques indicated the advantages of metal chelate interaction chromatography over ion exchange chromatography under the conditions examined.
Applications of the chicken IgG isolated by metal chelate interaction chromatography to an enzyme-linked immunosorbent assay for the detection of β-N-acetylglucosaminidase was attempted. Linear relationships were obtained when standard solutions of the enzyme were used in the assay. The results indicate that MCIC-isolated chicken immunoglobulins have excellent potential for use in analytical tests. / Land and Food Systems, Faculty of / Graduate
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Derivation of monoclonal antibodies to ferredoxin from Clostridium pasteurianumWeaver, Michael Stanley January 1980 (has links)
Modifications to the standard techniques of somatic cell fusion are presented which have resulted in the derivation of hybrid cell lines secreting monoclonal antibody to the low molecular weight antigen ferredoxin. Antibody secreted by one of these lines has been purified using the technique of protein. A sepharose chromatography. Using standard immunochemical methods it has been determined that this monoclonal antibody has an approximate isoelectric
pH of 8.5 - 8.6 and belongs to the IgG₂[sub b] subclass of immunoglobulin. / Science, Faculty of / Microbiology and Immunology, Department of / Graduate
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Immunochemical studies of myoglobin with synthetic peptides.Givas, Joan Katherine. January 1971 (has links)
No description available.
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