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Medicinal-Pharmaceutical Chemistry Commons

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Full-Text Articles in Medicinal-Pharmaceutical Chemistry

A Prostaglandin Synthase Inhibition Assay With Detection By Elisa, Patricia Scott Apr 1990

A Prostaglandin Synthase Inhibition Assay With Detection By Elisa, Patricia Scott

Theses, Dissertations & Honors Papers

A simple, reliable method is described for the routine measurement of non-steroidal anti-inflammatory drugs (NSAIDs) as inhibitors of prostaglandin synthase. Appropriate concentrations of inhibitor are incubated with ram seminal vesical prostaglandin synthase, sodium arachidonate and reduced glutathione. Prostaglandin E2 (PGE2) production is then quantitated by and enzyme linked immunosorbant assay (ELISA), in which anti-PGE2 antibody is utilized in a binding competition between test sample and adsorbed conjugate of PGE2-BSA. The antibody which remains bound to the solid phase is quantitatively determined colorimetrically by incubation with horse radish peroxidase labeled goat anti-rabbit IgG followed by incubation ...


Telomere Structure In Euplotes Crassus: Characterization Of Dna-Protein Interactions And Isolation Of A Telomere-Binding Protein, Carolyn M. Price Jan 1990

Telomere Structure In Euplotes Crassus: Characterization Of Dna-Protein Interactions And Isolation Of A Telomere-Binding Protein, Carolyn M. Price

Faculty Publications -- Chemistry Department

The nucleoprotein structure of telomeres from Euplotes crassus was studied by using nuclease and chemical footprinting. The macronuclear telomeres were found to exist as DNA-protein complexes that are resistant to micrococcal nuclease digestion. Each complex encompassed 85 to 130 base pairs of macronuclear DNA and appeared to consist of two structural domains that are characterized by dissimilar DNA-protein interactions. Dimethyl sulfate footprinting demonstrated that very sequence-specific and salt-stable interactions occur in the most terminal region of each complex. DNase I footprinting indicated that DNA in the region 30 to 120 base-pairs from the 5' end lies on a protein surface ...