Thesis (M.S.)--University of Wisconsin--Madison. / Typescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 43-47).

Thesis (M.S.)--University of Wisconsin--Madison. / Typescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 59-69).

The antral hormone gastrin has generally been regarded as a non antigenic molecule necessitating its conjugation with a large "carrier” to be an effective inducer of antibody. Such conjugation has normally taken the form of covalent binding to a highly antigenic molecule or ionic binding to an inert particle. Alternatively, some success has been achieved by the injection of impure antral extracts. This report describes four approaches to the problem of the induction of antibodies specific for gastrin. Initially, natural hog gastrin was obtained after the procedure of Gregory and Tracy (1964). The pure active hormone was modified by alkaline hydrolysis to liberate an N-terminal amino group for covalent conjugation. The modified gastrin, however, was not specifically identified or isolated in quantity. Consequently, pure and impure antral extracts, hemocyanin-bound synthetic human gastrin and latex-bound gastrin were applied to a variety of animals. Passive hemagglutination tests in ducks revealed titres of 400 to 1600 to both the pure and impure extracts but a series of four injections of pure gastrin into an antrectomized rabbit failed to raise detectable antibody. Injections of 3 mg. of SHG bound to hemocyanin was unsuccessful; antibody titre to the carrier molecule was high but no specificity appeared to be directed to the synthetic hapten. The immunization of chickens with latex-bound natural gastrin was more fruitful. Although a number of precipitin tests established the presence of antibodies to gastrin, it was apparent that the assay was inadequate as a sensitive test for the bivalent antigen. Furthermore, the antibody titre was not sufficiently high to be successfully applied to a radioimmunoassay. / Medicine, Faculty of / Cellular and Physiological Sciences, Department of / Graduate

The investigation presented here was accomplished using agglutination and agar gel immunodiffusion techniques to compare Azotobacter agilis s 3at, A. chroococcum Italy AC 16, A. macrocytogenes St. M and A. vinelandii ATCC 12837. It was found that the agglutination titers differed sufficiently to allow partial identification of the four species. The homologous and heterologous systems studied by agar gel immunodiffusion tests showed that each of the four Azoto bacter species differed sufficiently in their soluble antigens to give distinct, identifiable patterns of antigen-antibody reactions on Ouchterlony agar plates. These studies also showed several antigens common to the four species tested and the resultant antigen-antibody cross reactions. The results of these investigations suggest that this approach opens a new avenue for the identification of the organisms of genus Azotobacter and perhaps, by extension, the family Azotobacteraceae.

Thesis--University of California. / eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.

Thesis--Copenhagen. / "Oversigt": p. [166]-170. "References": p. [171]-172.

Thesis--University of California. / Includes bibliographical references.

Thèse--Liège. / Includes bibliography.

Thèse--Liège. / Includes bibliography.

In animals immunized with 2,4 dinitrophenyl (DNP) hapten-carrier protein conjugates, no in vitro cellular response is elicited by DNP, either alone, or when coupled to a heterologous carrier. In contrast, animals immunized with haptenic peptide-carrier conjugates do mount an in vitro cellular response towards the haptenic peptide. This apparent inconsistency led us to compare the in vivo and in vitro cellular immune responses to a synthetic peptide antigen and its DNP derivative to determine the activation specificity of the cells evoking this response. Guinea pigs were immunized with either the DNP substituted immunogen (DNP-N-10-C) or its unsubstituted form (N-10-C) and subsequent in vivo or in vitro cellular activation was evaluated for DNP alone, DNP coupled to the homologous determinant, and DNP coupled to heterologous carriers. The data suggests that in DNP-N-10-C immune guinea pigs, DNP substitution opens a new determinant exhibiting, in antigen reactive cells, a unique specificity towards the DNP moiety as well as a portion of the peptide to which it is conjugated. However the DNP group by itself does not have the configurational requirement to evoke cellular activation. It therefore plays a minor role in activation of the cellular immune response; the major contribution being supplied by the peptide portion of the 'shared' determinant. / Science, Faculty of / Microbiology and Immunology, Department of / Graduate