Typescript. / Thesis (Ph. D.)--University of Hawaii, 1968. / Bibliography: leaves [147]-155. / xiv, 155 l illus., tables

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Typescript. / Thesis (Ph. D.)--University of Hawaii, 1969. / Bibliography: leaves 148-154. / xii, 154 l illus

Ferredoxin (Fd), a fifty-five amino acid electron transport protein of the anaerobe Clostridium pasteurianum, has been chosen as the ideal probe for immunoregulation studies. Its critical feature is that it contains two antigenic determinants satisfying the hypothetical minimum requirement for immunogenicity. It was found that both the antibody (as measured by ELISA) and the lympho-proliferative responses to Fd are linked exclusively to the MHC of mice, mapping to K/I-A. Analysis of the response was undertaken at the determinant level with selective enzyme cleavage products of trypsin and carboxypeptidase A which yield respectively a 52 residue C-determinant peptide (devoid of a functional N-determinant), "C", and a 53 residue N-determinant peptide (devoid of a functional C-determinant peptide), "N",. Through the use of these two molecules ("N" and "C") and a doubly digested molecule, "M", the immune response to Fd was dissected. At first, anti-Fd antibody from high responder, H-2[sup=k], mice was shown to be 10-20% "N" specific with the balance of the response "C" directed, while intermediate responder haplotypes, H-2[sup=b] and H-2[sup=s]. demonstrate equal specificity for the two determinants. H-2 mice were uniformly non-responsive. Fd immune T-cells demonstrated lymphoproliferative capacity mirroring the antibody response of B10.BR (H-2[sup=k]) mice: "C" induced proliferation comparable to that with the native molecule, "N" inducing a much lower response, one matched by the "M" peptide. Next, the "N", "C" and "M" molecules were assessed for their immunogenicity in B10.BR, C57BL/10 (H-2[sup=b])and B10.D2 (H-2[sup=d]) mice. "N" was found to induce limited, if any, antibody production whereas it primes for a very good proliferative response (B10.BR only). "M" induced no antibody response in any strain, and minimal proliferation in B10.BR. "C" induced at least two-fold higher antibody in B10.BR and C57BL/10 as compared to native Fd, and converted the B10.D2 non-responders into responders. "C" induced a weak proliferative response in B10.BR. The data suggest that two determinants exist at the B-cell level, while three determinants account for the T-cell response. / Science, Faculty of / Microbiology and Immunology, Department of / Graduate

Anti-idiotype antisera were raised in rabbits to two monoclonal antibodies, Fd-1 and Fd-2, with specificity for each of the two antigenic epitopes found on the ferredoxin (Fd) molecule. The anti-idiotype antisera (anti-Fd-1 and anti-Fd-2) were used to demonstrate that one of the idiotypes (Fd-1) was expressed at significant levels in most anti-Fd antisera raised in BIO.BR mice while the second idiotype (Fd-2) was infrequently expressed. Examination of anti-Fd sera raised in other mouse strains demonstrated that expression of the Fd-1 idiotype mapped to the IgH gene complex and was found in the antisera of all mouse strains examined with the Ig-1[sup=b] allotype. When splenocytes from Fd-immune B10.BR mice were treated with anti-Fd-1 and transferred to irradiated syngeneic recipients, the adoptive secondary response was significantly higher in animals receiving treated cells as opposed to control animals which received normal rabbit serum treated cells. This response produced a net increase in antibody to both epitopes and the relative amount of Fd-1 idiotope was not significantly altered. Further studies with separated cell populations showed that the overall increase of anti-Fd antibody produced was attributable to the effects of the anti-idiotypic serum on a population(s) of T cells. Treatment of mice with the Fd-1 monoclonal antibody (which should react with anti-idiotypic cells) had an analogous effect to that of the anti-idiotype. Treated mice produced heightened levels of antibodies directed to both epitopes of Fd. Treatment of mice with second anti-idiotype, anti-Fd-2, was found to enhance the anti-Fd response of B10.BR mice and abrogate the non-responder status of DBA/2 mice. Additional evidence indicates that the Fd-2 idiotype could be expressed on a suppressor cell population which may be a predominant regulatory element in both BIO.BR and DBA/2 mice. / Science, Faculty of / Microbiology and Immunology, Department of / Graduate

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Thesis (PhD)--Montana State University--Bozeman, 2009. / Typescript. Chairperson, Graduate Committee: C. Martin Lawrence. Includes bibliographical references (leaves 101-112).

Universiẗat, Diss., 2002--Frankfurt (Main).

Zugl.: Diss.

In higher plants, [2Fe-2S] cluster containing fererdoxins (Fds) are the unique electron acceptors from photosystem I (PSI). Fds are small, soluble proteins and distribute these electrons to many enzymes, which act in different metabolic and signaling pathways. In addition to four well studied Fds, Arabidopsis possess genes for two significantly different, as yet uncharacterized Fds, with extended C-terminals, which are therefore called FdCs. For normal Fds, this C-terminus is critical for interaction with the C, D and E subunits of PSI during photosynthetic electron transport (PET). FdC1 and FdC2 are highly conserved from algae and cyanobacteria respectively to higher plants. This leads to the suggestion that they fulfill a conserved function, which is so far unknown. The results presented in this thesis show that FdC1 is a chloroplast located protein with a [2Fe-2S] cluster showing a blue shift in the electron paramagnetic resonance (EPR) spectrum in comparison to the well-known Fds. The EPR g values of FdC1 point to high similarity with the organization of the succinate dehydrogenase [2Fe-2S] cluster than that of classical Fd clusters. Furthermore it was established that FdC1 is unlikely to be involved in PET, due to its inability to photoreduce NADP+, because of a more positive redox potential in comparison to the well-studied Fds. In several interaction studies no previously described Fd-dependent enzymes could be found. By contrast FdC1 was found to interact with two of five enzymes of sulfate assimilation, serine O-acetyltransferase 2;1 (SERAT2;1) and 3‘-phosphoadenosine 5‘-phosphosulfate synthase (APS3), and it is proposed that FdC1 might have a regulatory function in sulfur assimilation through its interaction with these two proteins. Furthermore, several redox enzymes were found to interact with FdC1. One of these enzymes is the 3-oxoacyl-[acyl-carrier-protein] reductase, which is part of the fatty acid synthase complex. This interaction opens up the question, whether FdC1 might be able to channel electrons into the synthesis of specific fatty acids. In case of FdC2 the results have also proven that it is a chloroplast located protein containing a [2Fe-2S] cluster. FdC2 was detected in defined foci in the chloroplast, and our data suggests that in is both soluble and localized at the chloroplast envelope membrane. FdC2 is also very unlikely to be involved in PET, because it was found to be unable to receive electrons from PSI or FNR. Furthermore it is proposed that FdC2 has an alternative function in copper (Cu) import into the chloroplast through interaction with a Cu transporting ATPase, PAA1. This interaction was confirmed by several methods, although its functional significance is not yet completely understood. One possibility is that FdC2 regulates PAA1 or supports the reduction of Cu2+ to Cu+, before import into the chloroplast is possible.