831 research outputs found
Encouragement sermon notes
John W. Goodwin\u27s outline and notes for sermon entitled Encouragement. The typescript of the sermon outline also includes pencil annotations and blue and pink highlighting. The date of creation is estimated to be circa 1965
For the People had a Mind to Work sermon notes
John W. Goodwin\u27s outline and notes for the sermon For the People had a Mind to Work. The typescript outline includes hand written annotations and blue and pink highlighting. The date of creation is estimated to be circa 1965
Fools Make a Mock of Sin sermon notes
John W. Goodwin\u27s outline and notes for his sermon Fools Make a Mock of Sin. The typescript outline has had written annotations and blue and pink highlighting. The date of creation is estimated to be 1965
Hydrogen Peroxide Inhibition of Bicupin Oxalate Oxidase
Oxalate oxidase is a manganese containing enzyme that catalyzes the oxidation of oxalate to carbon dioxide in a reaction that is coupled with the reduction of oxygen to hydrogen peroxide. Oxalate oxidase from Ceriporiopsis subvermispora (CsOxOx) is the first fungal and bicupin enzyme identified that catalyzes this reaction. Potential applications of oxalate oxidase for use in pancreatic cancer treatment, to prevent scaling in paper pulping, and in biofuel cells have highlighted the need to understand the extent of the hydrogen peroxide inhibition of the CsOxOx catalyzed oxidation of oxalate. We apply a membrane inlet mass spectrometry (MIMS) assay to directly measure initial rates of carbon dioxide formation and oxygen consumption in the presence and absence of hydrogen peroxide. This work demonstrates that hydrogen peroxide is both a reversible noncompetitive inhibitor of the CsOxOx catalyzed oxidation of oxalate and an irreversible inactivator. The build-up of the turnover-generated hydrogen peroxide product leads to the inactivation of the enzyme. The introduction of catalase to reaction mixtures protects the enzyme from inactivation allowing reactions to proceed to completion. Circular dichroism spectra indicate that no changes in global protein structure take place in the presence of hydrogen peroxide. Additionally, we show that the CsOxOx catalyzed reaction with the three carbon substrate mesoxalate consumes oxygen which is in contrast to previous proposals that it catalyzed a non-oxidative decarboxylation with this substrate
Optimum Distribution Patterns for Feeder Cattle
The Oklahoma Agricultural Experiment Station periodically issues revisions to its publications. The most current edition is made available. For access to an earlier edition, if available for this title, please contact the Oklahoma State University Library Archives by email at [email protected] or by phone at 405-744-6311
Irreversible Demand Function for Beef
The Oklahoma Agricultural Experiment Station periodically issues revisions to its publications. The most current edition is made available. For access to an earlier edition, if available for this title, please contact the Oklahoma State University Library Archives by email at [email protected] or by phone at 405-744-6311
Aggregation of Normative Microsupply Relationships for Dryland Crop Farms in the Rolling Plains of Oklahoma and Texas
The Oklahoma Agricultural Experiment Station periodically issues revisions to its publications. The most current edition is made available. For access to an earlier edition, if available for this title, please contact the Oklahoma State University Library Archives by email at [email protected] or by phone at 405-744-6311
Carotenoid biosynthesis in a Flavobacterium sp.: stereochemistry of hydrogen elimination in the desaturation of phytoene to lycopene, rubixanthin and zeaxanthin (Short Communication)
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