Open Access. Powered by Scholars. Published by Universities.®
- Discipline
Articles 1 - 4 of 4
Full-Text Articles in Life Sciences
Characterization Of Two Temperature-Sensitive Mutants Of Escherichia Coli Exhibiting An Altered L22 Ribosomal Protein, Bonnie A. Burnette-Vick
Characterization Of Two Temperature-Sensitive Mutants Of Escherichia Coli Exhibiting An Altered L22 Ribosomal Protein, Bonnie A. Burnette-Vick
Electronic Theses and Dissertations
Analysis of E. coli strains SK1047 and SK1048 have shown them to be temperature-sensitive, protein-synthesis deficient. An alteration in ribosomal protein L22 was detected in both strains using two dimensional gel electrophoresis. Protein L22 was purified from both strains by reversed phase high performance liquid chromatography and from two dimensional electrophoretic gels. Purified ribosomal protein L22 was labeled by reductive methylation and used in 23S RNA binding assays with and without ribosomal protein L4. At the permissive temperature, protein L22 from SK1047 bound less efficiently than the control while protein L22 from SK1048 bound as efficiently as the control. At …
Mouse Mast Cell Proteases: Induction, Molecular Cloning, And Characterization, Wei Chu
Mouse Mast Cell Proteases: Induction, Molecular Cloning, And Characterization, Wei Chu
Electronic Theses and Dissertations
Tryptase, a mast cell-specific serine protease with trypsin-like specificity, has been identified in a mouse mast cell line (ABFTL-6) based on it's enzymatic activity, inhibition properties, and cross-reactivity to a human mast cell tryptase antibody. The effects of fibroblast-conditioned medium and sodium butyrate on ABFTL-6 mast cell differentiation and tryptase expression have been examined. ABFTL-6 mouse mast cells undergo phenotypic changes upon culturing in media supplemented with fibroblast-conditioned media at 50% or 1 mM sodium butyrate. The induced cells increased in size, had larger and more metachromatic cytoplasmic granules, and increased their total cellular protein about four-fold. Tryptase activity increased …
Nitrogen Dioxide Reaction With Proteins: Evidence For Peptide Bond Cleavage At Lysine Residues, Darryl B. Hood
Nitrogen Dioxide Reaction With Proteins: Evidence For Peptide Bond Cleavage At Lysine Residues, Darryl B. Hood
Electronic Theses and Dissertations
Nitrogen dioxide (NO$\sb2$), an air pollutant produced by burning fossil fuels and a component of cigarette smoke, is thought to contribute to the pathogenesis of pulmonary diseases, such as emphysema. To gain information on the mechanism by which NO$\sb2$ damages the lung, in vitro exposures of $\alpha\sb1$-proteinase inhibitor ($\alpha\sb1$-PI), elastin, bovine serum albumin (BSA), human serum albumin (HSA) and synthetic poly-L-lysine were performed. A genetic deficiency of $\alpha\sb1$-PI predisposes humans to emphysema and NO$\sb2$ has been hypothesized to damage $\alpha\sb1$-PI, which would leave proteases such as human neutrophil elastase, (HNE) free to attack lung structural proteins. The ability of $\alpha\sb1$-PI …
Metabolism Of Arachidonate-Containing Phospholipid Molecular Species In The Murine Macrophage-Like Cell Line, P388d1, Crystal R. Waites
Metabolism Of Arachidonate-Containing Phospholipid Molecular Species In The Murine Macrophage-Like Cell Line, P388d1, Crystal R. Waites
Electronic Theses and Dissertations
Glycerophospholipids of mammalian cells exist as chemically diverse structures with various fatty acids at the sn-1 and sn-2 positions. Arachidonic acid, a polyunsaturated fatty acid, which may be converted to biologically active eicosanoids such as prostaglandins, thromboxanes, and leukotrienes, is found predominantly in the sn-2 position of glycerophospholipids. The purpose of this study was to examine, at the level of the individual molecular species, the incorporation of arachidonate into phospholipids and its release from phospholipids during stimulation. In this way, the specificity of the enzymes controlling arachidonate metabolism could be examined in order to clarify the processes that control the …