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Characterization by optical methods of the heat denaturation of bovine serum albumin (BSA) as affected by protein concentration, pH, ionic strength and sugar concentration /Kongraksawech, Teepakorn. January 1900 (has links)
Thesis (M.S.)--Oregon State University, 2007. / Printout. Includes bibliographical references (leaves 92-98). Also available on the World Wide Web.
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Influence of twenty-five per cent human serum albumin on total and ionized calcium concentrations in vivoErstad, Brian L., Richards, Hal, Rose, Susan, Nakazato, Paul, Fortune, John January 1999 (has links)
BACKGROUND:A inverse correlation has been found between changes in ionized calcium concentrations and the addition of albumin in vitro, which may explain adverse cardiovascular effects attributed to exogenous albumin in vivo. The purpose of this investigation was to determine the interaction (if any) between exogenous 25% albumin administration (100 ml given over < 30 min) and calcium concentrations in patients, all but one of whom were in an intensive care unit.RESULTS:There were no significant differences in the ionized calcium concentrations obtained before, at the end and 6 h after the administration of albumin (1.09 +/- 0.23, 1.06 +/- 0.22, 1.06 +/- 0.21 mmol/l, respectively). Similarly, there were no significant differences in the total calcium concentrations between these same time periods (2.03 +/- 0.18, 2.05 +/- 0.20, 2.08 +/- 0.23 mmol/l, respectively).CONCLUSIONS:In patients receiving infusions of 25% albumin, it appears that circulating calcium concentrations are well regulated by homeostatic mechanisms. Albumin infusions had no effect on calcium concentrations, although it is possible that temporary changes of questionable clinical importance may have occurred between measurement periods.
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FLUORESCENCE AND THE STRUCTURES OF SERUM ALBUMINS.ELSHEIKH, FATHELRAHMAN ABBAS. January 1987 (has links)
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.
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Studies on the non-enzymatic glucosylation of human proteinBrighton, M. W. January 1987 (has links)
No description available.
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Albumin-like proteins of the Atlantic salmon, Salmo salar, and rainbow trout, Oncorhynchus mykissLakehal, Ferhat January 1997 (has links)
No description available.
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Characterization of Cys-34 in serum albuminTong, Grace C., January 2003 (has links)
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).
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The relationship between serum albumin and effective osmolality during the progression of dehydration in female ratsTierney, Kathleen T. January 1999 (has links)
There is no abstract available for this thesis. / Department of Family and Consumer Sciences
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Studies on serum albumin and hemoglobin the two principal transport proteins in blood /Fang, Yunnan. January 2004 (has links)
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
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The adsorption of bovine serum albumin on fused silica : a single molecules studyYeung, Kai Ming 01 January 2008 (has links)
No description available.
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Polymerized serum albumin beads for use as slow-release adjuvantsMartin, Michelle Elizabeth Denny January 1988 (has links)
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.
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