Thesis (M.S.)--Oregon State University, 2007. / Printout. Includes bibliographical references (leaves 92-98). Also available on the World Wide Web.

The perturbation of fluorescence in both bovine and human serum albumin caused by chloride, iodide, acrylamide and N-bromosuccinimide was studied under various experimental conditions. Serum albumin fluorescence lifetime changes induced by pH and added solutes were also studied, both in acid solutions and in powders. In general, the two proteins behave similarly. During the N-F transitions, the fluorescence lifetimes and the fluorescences intensities decrease in the same qualitative manner. Chloride binding enhances the fluorescence intensity, but has little or no effect on the fluorescence lifetimes. Chloride enhances the human serum albumin fluorescence intensity much more than it enhances that of bovine serum albumin. Iodide and acrylamide quench both the fluorescence intensities and lifetimes. Acrylamide quenching is hardly affected by pH changes, but is sensitive to the protein concentration. In acrylamide quenching, acrylamide molecules are partitioned into the protein matrix, causing both dynamic and static quenching. Iodide quenching is sensitive to pH, with a maximum quenching at pH 4.0. Iodide quenching decreases with increased ionic strength and with increased protein concentration. The Stern-Volmer plots obtained with iodide as the quencher are downward curving in both proteins. The downward curvature is a result of iodide binding, the main quenching mechanism. Both tryptophans in bovine serum albumin tryptophans and the single human serum albumin tryptophan are very close to the surface of the protein. The environments of the bovine serum albumin tryptophans are not very different from each other. The fluorescence lifetimes of serum albumin powders separated at pH 6.0 are very sensitive to hydration, while the lifetimes of powders separated at pH 2.0 are not. Acrylamide and iodide quench the fluorescence lifetimes of bovine serum albumin powders, even in the driest samples. Quenching is maximum at a hydration approximately equal to that required for monolayer coverage.

Thesis (Ph. D.)--Ohio State University, 2003. / Title from first page of PDF file. Document formatted into pages; contains xxiii, 325 p.; also contains graphics (some col.). Includes abstract and vita. Advisor: Gary E. Means, Dept. of Biochemistry. Includes bibliographical references (p. 206-225).

There is no abstract available for this thesis. / Department of Family and Consumer Sciences

Thesis (Ph. D.)--Ohio State University, 2004. / Title from first page of PDF file. Document formatted into pages; contains xviii, 133 p.; also includes graphics (some col.). Includes bibliographical references (p. 121-133). Available online via OhioLINK's ETD Center

No description available.

Experimental vaccines have been made by covalently bonding virus particles into polymerized rabbit serum albumin beads. Using Nodamura virus as a model antigen, these model vaccines induced specific humoral antibody production, comparable with that achieved using Freund's adjuvants. Virus specific antibodies were also induced when Nodamura virus was covalently attached to the bead surface using different crosslinkers. However, when poliovirus type 2 (Sabin strain) was polymerized into beads, the levels of neutralizing antibodies were insignificant compared with control aqueous vaccines. The synthetic immunostimulator, muramyl dipeptide, was included with bead vaccines in an attempt to potentiate the immune response. Immunostimulation is achieved by a slow release of antigen coinciding with the gradual breakdown of bead structure.

Lee, T. et al (1981) proposed the encapsulation of hormones such as progesterone into serum albumin beads, such that their in vivo proteolysis would allow a gradual release of hormone at low levels, for extended hormone action. It was proposed, in the Department of Microbiology, Rhodes University, to replace the hormone component of the above bead formulation, with virus as antigen, in the development of a vaccine. Beads optimally crosslinked at 1% final glutaraldehyde concentration, containing Nodamura virus, were shown to promote an adjuvant effect in vivo, analogous to the release of antigen from Freund's Complete Adjuvant (FCA), so that extended immunostimulation resulted. It was shown that soluble antigen promoted a short-lived primary immune response, peaking around day 25 following inoculation. Antigen presented in beads, on the other hand, initially elicited a low humoral response, but this response gradually increased up to a peak around day 110 post inoculation, before decreasing. No apparent adverse side-effects were noted following inoculation of antigen-containing serum albumin beads, compared to necrosis following antigen in FCA inoculation, supporting the proposal of using albumin homotypic for the test inoculee animal, so that the beads would themselves be non-immunogenic and would merely act as a vehicle in the vaccine formulation. The indirect enzyme-linked immunosorbent assay (ELISA) was used to monitor the humoral response to antigen following inoculation. Results showed that covalent crosslinking of albumin in the formation of the beads did not promote immunogenicity on the part of the chemically altered albumin. The ELISA test was used to indicate the kinetics of the IgG response to Nodamura virus when presented in formulations such as: Freely soluble virus or its subunit; soluble intact virus inactivated by treatment with glutaraldehyde; intact virus entrapped in serum albumin beads cross; linked at different percentage final glutaraldehyde concentrations and also virus subunit prepared in albumin beads. The presence of virus-neutral ising antibodies was noted in serum obtained from rabbits inoculated with virus entrapped in albumin beads. Virus infectivity, titrated in mice, showed protection against virus challenge after incubation of virus with serum obtained above.

No description available.

Thesis--Copenhagen. / Summary in Danish. Includes bibliographical references (p. 175-191).