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The electrophoretic behavior of sarcoplasmic proteins was investigated by the use of vertical acrylamide gel electrophoresis. The first part of the study was concerned with the separation of sarcoplasmic proteins extracted at different times of post-mortem aging. Electrophoresis of the sarcoplasmic extracts by the discontinuous technique, using ten percent acrylamide gels, resulted in the separation of 18 (possibly 20) electrophoretically different proteins. Differences between electrophoretic patterns of sarcoplasmic proteins as post-mortem aging proceeded were slight. Heterogeneity of sarcoplasmic protein fractions obtained by DEAE-cellulose chromatography was investigated by vertical acrylamide gel electrophoresis in the second part of this study. Electrophoretic analyses of the sarcoplasmic fractions from the above separations indicated that the major peaks of the chromatographic profiles were quite heterogeneous. Fraction Areas I and IV, which appeared as single homogeneous chromatographic peaks, showed five and six distinct bands, respectively, when subjected to gel electrophoresis. Once again changes in the electrophoretic patterns at 0 and 10 days of post-mortem aging were slight with main differences being in the density of the bands. The versatility and high resolving power of acrylamide gel electrophoresis for separating sarcoplasmic proteins was demonstrated. Excellent reproducibility of electrophoretic patterns was noted and in most instances, the patterns were clear and showed well-defined bands. Attempts to fractionate sarcoplasmic proteins by density gradient electrophoresis resulted in separations characterized by poor resolution. / Graduation date: 1968

Graduation date: 1970

Graduation date: 1971

Cold shock proteins (Csp) are small acidic proteins that fold into ??-barrel structures with five anti-parallel ??-strands and are involved in essential cellular processes. Upon temperature downshift the synthesis of Csp proteins is drastically increased to enable cells to restore growth in the cold. These proteins facilitate transcription and translation at low temperature by functioning as RNA chaperones. Csp proteins have been most extensively studied in Bacteria but very few Csp homologues have been identified and studied in Archaea. This is the first study examining structural, functional and biophysical properties of Csp from the Antarctic archaeon Methanogenium frigidum. The fastidious growth requirements of M. frigidum make it difficult to cultivate, therefore recombinant methods have been developed for the expression and characterization of the protein. The analysis by transverse urea gradient gel electrophoresis (TUG-GE) revealed that M. frigidum Csp folds by a reversible two-state mechanism and has a low conformational stability. The spectroscopic analysis of the protein performed by Circular Dichroism (CD) spectroscopy disclosed features typical of other homologous proteins. A possible association between Csp and RNA has been proposed according to MALDI-TOF mass spectrometry analysis. The effect of a Nterminal polyhistidine affinity tag on the biophysical properties of Csp was also examined. The biological activity of Csp was investigated by complementation of an E. coli cold sensitive mutant. These studies revealed that the M. frigidum Csp is biologically active and can function in E. coli.

140 p. / Title page, contents and abstract only. The complete thesis in print form is available from the University Library. / The aim of the work described in this thesis was to isolate the gene encoding a protein involved in the generation of Early Pregnancy Factor (EPF) activity. EPF activity is defined as the ability of pregnancy serum to induce a positive response in the rosette inhibition test (RIT). Non-pregnant serum fails to give a positive response in this assay and therefore does not containe EPF activity. / Thesis (Ph.D.)--University of Adelaide, Dept. of Biochemistry. 1990

The ubiquitin pathway is a highly conserved post-translational modification system best characterised for its roles in protein degradation and intracellular trafficking and is involved in a diverse spectrum of cellular processes. Ubiquitylation is opposed by deubiquitylating enzymes (Dubs), and the ubiquitin specific peptidase (USP) class of Dubs remove ubiquitin from specific substrates, thereby affecting protein fate. USPs exhibit broad sequence diversity except over their catalytic cores and it has been suggested that this sequence variation constitutes their individual substrate-specific binding sites. Fat Facets in Mouse (Fam) is a developmentally regulated USP whose function is crucial for mouse pre-implantation development. Fam is expressed in a complex fashion throughout development in a number of diverse tissue types and time points, well beyond its critical role in the early embryo. Fam's orthologue in fly, Fat Facets (faf) is also developmentally regulated and is required for both drosophila eye and syncytial stage development. Given the strengths of the zebrafish system as a developmental tool, the zebrafish orthologue of Fam, usp9 was identified and found to be highly conserved. Analysis of its expression pattern found considerable overlap with the published mouse patterns. Given the similarities between the mouse and zebrafish systems, a series of cross-species experiments were conducted to determine whether exogenous expression of highly conserved regions of FAM, could cause dominant-negative phenotypes in developing zebrafish embryos. Outside of the catalytic core, FAM's large N and C-terminal extensions consist of novel sequence bearing no similarity to any known domain. To delineate FAM domains, fulllength FAM was expressed in insect cells and subjected to partial proteolysis. Combining this data with recent structural predictions and computer analyses of the FAM sequence, four FAM domains were characterised with the first domain containing three possible subdomains. The predominant helical nature of the N and C-terminal extensions of FAM were predicted to form scaffolding structures, well suited to protein binding. / Thesis (M.Sc.)-- University of Adelaide, School of Molecular and Biomedical Science, 2006.

Thesis (doctoral)--University of Uppsala. / Issued also as: Nova Acta Regiae Societatis Scientiarum Upsaliensis ; ser. IV, v. 7, n:o 4. Includes bibliographical references (p. 103-105).

Thesis (Ph.D.)--Tufts University, 2000. / Adviser: David L. Kaplan. Submitted to the Dept. of Biotechnology Engineering. Includes bibliographical references. Access restricted to members of the Tufts University community. Also available via the World Wide Web;

Thesis (M.S.)--George Mason University, 2007. / Title from PDF t.p. (viewed Jan. 22, 2008). Thesis director: V. Rao Mulpuri. Submitted in partial fulfillment of the requirements for the degree of Master of Science in Electrical Engineering. Vita: p. 49. Includes bibliographical references (p. 43-48). Also available in print.