Publications (48) View all
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Dataset: Amidinotransferase FEBS2012
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Article: Proteomic assessment of host-associated microevolution in the fungus Thielaviopsis basicola.
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ABSTRACT: Thielaviopsis basicola, a soil-borne pathogen with a broad host range and a cosmopolitan distribution, is emerging as a major risk to sustainable cotton production in Australia. Previous studies suggested that host specialization has occurred making T. basicola an ideal model for a comparative proteomic analysis of strains isolated from different hosts. Elucidation of the genomic diversity and investigation of the functional differences in the Australian population could provide valuable information towards disease control. In this study, isolates of T. basicola were investigated for genomic (internal transcribed spacers region), proteomic and cotton virulence level variations. Internal transcribed spacers sequence analysis revealed that isolates are grouped based on host of origin irrespective of geographical origin. At the proteome level a degree of diversity was apparent and hierarchical clustering analysis of the data also demonstrated a close correlation between the proteome and the host of origin. LC-MS/MS analysis and identification using cross-species similarity searching and de novo sequencing of host-specific differentially expressed proteins and the virulence-correlated proteome allowed successful identification of 43 spots. The majority were found to be involved in metabolism. Spots that were correlated with host and virulence differences included a hypothetical protein with a Rossman-fold NAD(P)(+)-binding protein domain, glyceraldehyde-3-phosphate dehydrogenase, arginase and tetrahydroxynaphthalene reductase.Environmental Microbiology 10/2010; 13(3):576-88. · 5.84 Impact Factor -
Article: A novel approach for enhancing the catalytic efficiency of a protease at low temperature: reduction in substrate inhibition by chemical modification.
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ABSTRACT: The alkaline protease, savinase was chemically modified to enhance the productivity of the enzyme at low temperatures on a complex polymeric protein (azocasein) substrate. At 5 and 15 degrees C, savinase modified with ficol or dextran hydrolyzed fivefold more azocasein than the unmodified savinase. Kinetic studies showed that the catalytic improvements are associated with changes in uncompetitive substrate inhibition with K(i) values of modified savinases sixfold higher than the unmodified savinase. Modeling of small-angle scattering data indicates that two substrate molecules bind on opposing sides of the enzyme. The combined kinetic and structural data indicate that the polysaccharide modifier sterically blocks the allosteric site and reduces substrate inhibition. In contrast to the properties of cold-active enzymes that generally manifest as low activation enthalpy and high flexibility, this study shows that increased activity and productivity at low temperature can be achieved by reducing uncompetitive substrate inhibition, and that this can be achieved using chemical modification with an enzyme in a commercial enzyme-formulation.Biotechnology and Bioengineering 03/2009; 103(4):676-86. · 3.95 Impact Factor -
Chapter: Inflammatory, oxidative and vascular factors affecting neuronal cell death in Alzheimer’s disease
01/2006; , ISBN: 159454929X -
Article: Recovery of peptides and proteins following matrix‐assisted laser desorption/ionization mass spectrometry
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ABSTRACT: Only attomole quantities of polypeptide are consumed during analysis by matrix-assisted laser desorption/ionization, despite the need to load picomole quantities of these analytes onto the target. By using radioimmunoassay we have demonstrated that the balance of the material (i.e., effectively all that was loaded onto the slide) can be recovered from the target and remains in an immunoreactive form. The bulk of the material, once recovered from the target, can be examined by other analytical techniques including sodium dodecyl sulphate polyacrylamide gel electrophoresis.Rapid Communications in Mass Spectrometry 04/2005; 9(3):233 - 239. · 2.79 Impact Factor
