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1.
Inorg Chem ; 59(14): 9465-9470, 2020 Jul 20.
Artigo em Inglês | MEDLINE | ID: mdl-32584035

RESUMO

Two unprecedented organic amine templated silver organophosphonate hybrid solids have been synthesized hydrothermally by varying the molar ratio of the reactants. Both of the compounds consist of novel tetra- and penta-nuclear silver phosphonate basic building units. The dielectric constants are extremely large due to the charge separation of anionic metal phosphonate frameworks and cationic templated piperazine moieties in the compounds, as found for the first time in a hybrid organophosphate family. The conductivity and UV-visible absorption studies provide strong evidence about the semiconducting nature of the present compounds.

2.
J Chromatogr A ; 1216(20): 4372-6, 2009 May 15.
Artigo em Inglês | MEDLINE | ID: mdl-19168177

RESUMO

Increased recombinant protein expression yields and a large installed base of manufacturing facilities designed for smaller bulk sizes has led to the need for high capacity chromatographic resins. This work explores the impact of three pore sizes (with dextran distribution coefficients of 0.4, 0.53, and 0.64), dextran surface extender concentration (11-20mg/mL), and ligand density (77-138 micromol H+/mL resin) of cation exchange resins on the dynamic binding capacity of a therapeutic antibody. An intermediate optimal pore size was identified from three pore sizes examined. Increasing ligand density was shown to increase the critical ionic strength, while increasing dextran content increased dynamic binding capacity mainly at the optimal pore size and lower conductivities. Dynamic binding capacity as high as 200mg/mL was obtained at the optimum pore size and dextran content.


Assuntos
Anticorpos Monoclonais/isolamento & purificação , Resinas de Troca de Cátion/química , Cromatografia por Troca Iônica/métodos , Anticorpos Monoclonais/química , Dextranos/química , Concentração Osmolar , Tamanho da Partícula , Porosidade , Ligação Proteica
3.
Mol Cell Biol ; 27(7): 2466-75, 2007 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-17242192

RESUMO

Sir2 and Hst1 are NAD(+)-dependent histone deacetylases of budding yeast that are related by strong sequence similarity. Nevertheless, the two proteins promote two mechanistically distinct forms of gene repression. Hst1 interacts with Rfm1 and Sum1 to repress the transcription of specific middle-sporulation genes. Sir2 interacts with Sir3 and Sir4 to silence genes contained within the silent-mating-type loci and telomere chromosomal regions. To identify the determinants of gene-specific versus regional repression, we created a series of Hst1::Sir2 hybrids. Our analysis yielded two dual-specificity chimeras that were able to perform both regional and gene-specific repression. Regional silencing by the chimeras required Sir3 and Sir4, whereas gene-specific repression required Rfm1 and Sum1. Our findings demonstrate that the nonconserved N-terminal region and two amino acids within the enzymatic core domain account for cofactor specificity and proper targeting of these proteins. These results suggest that the differences in the silencing and repression functions of Sir2 and Hst1 may not be due to differences in enzymatic activities of the proteins but rather may be the result of distinct cofactor specificities.


Assuntos
Inativação Gênica , Histona Desacetilases/metabolismo , Proteínas de Saccharomyces cerevisiae/metabolismo , Saccharomyces cerevisiae/metabolismo , Proteínas Reguladoras de Informação Silenciosa de Saccharomyces cerevisiae/metabolismo , Sirtuínas/metabolismo , Sequência de Aminoácidos , Coenzimas/metabolismo , Proteínas de Ligação a DNA/metabolismo , Histona Desacetilases/genética , Dados de Sequência Molecular , Proteínas Nucleares/metabolismo , Estrutura Terciária de Proteína , Proteínas Repressoras , Saccharomyces cerevisiae/genética , Proteínas de Saccharomyces cerevisiae/genética , Homologia de Sequência de Aminoácidos , Proteínas Reguladoras de Informação Silenciosa de Saccharomyces cerevisiae/genética , Sirtuína 2 , Sirtuínas/genética
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