11 results match your criteria: "Washington Research Center[Affiliation]"

Organizational efforts to affirm sexual diversity: a cross-level examination.

J Appl Psychol

February 2001

Washington Research Center, American Institutes for Research, Washington, DC 20007-3541, USA.

A growing number of organizations have enacted policies intended to recognize and affirm sexual diversity in the workforce. This research demonstrates that the more prevalent these policies, the less likely sexual minority members are to experience treatment discrimination. Further, as expected, more equitable treatment was associated with higher levels of satisfaction and commitment among lesbian and gay employees.

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Agrobacterium tumefaciens strain 47C expresses an inducible D-hydantoinase that catalyzes the formation of optically pure N-carbamyl D-amino acids from racemic hydantoin precursors. The D-Hydantoinase was shown to be active and stable at elevated temperatures and pH values, thus affording favorable bioreaction conditions that result in the racemization of DL-hydantoins to the utilizable D-isomer. The enzyme demonstrated optimal reaction kinetics at pH 10 and 70 degrees C, was not activated by metal ions, and exhibited a distinctive substrate specificity.

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Novel biocarriers that combine the adsorptive properties of activated carbon with the ion-exchange properties of zeolite-based type Z inorganic oxide biocarriers (D. R. Durham, L.

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Inorganic matrices were developed for fixed-film bioreactors affording protection to microorganisms and preventing loss of bioreactor productivity during system upsets. These biocarriers, designated Type-Z, contain ion-exchange properties and possess high porosity and a high level of surface area, which provide a suitable medium for microbial colonization. Viable cell populations of 10/g were attainable, and scanning electron micrographs revealed extensive external colonization and moderate internal colonization with aerobic microorganisms.

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Vibriolysin, a proteolytic enzyme secreted by the marine microorganism Vibrio proteolyticus, was evaluated for its efficacy as an enzymatic debridement agent. Initial in vitro experiments revealed that the protease readily hydrolyzed proteinaceous components of eschar (e.g.

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The elastolytic properties of subtilisin GX from alkalophilic Bacillus sp. strain 6644 provides a means of differentiation from other subtilisins.

Biochem Biophys Res Commun

August 1993

W. R. Grace & Co.-Conn., Washington Research Center, Biological Chemistry Research Department, Columbia, MD 21044.

A serine protease exhibiting high activity in alkaline media was purified from alkalophilic Bacillus strain GX6644. The enzyme, subtilisin GX, has a molecular weight of 25,000 and a pI greater than 9.5.

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The gene (nprV), encoding the extracellular neutral protease, vibriolysin (NprV), of the Gram- marine microorganism, Vibrio proteolyticus, was isolated from a V. proteolyticus DNA library constructed in Escherichia coli. The recombinant E.

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Cell culture techniques were used to determine the source of cytotoxic agents in a commercial BIS-GMA composite. The material was polymerized according to the manufacturer's directions and leachable components were removed by room temperature extraction in ethanol, chloroform, or toluene. The leachable components in the extracts were identified using infrared spectrographic analysis.

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Identification of a distal regulatory element in the 5' flanking region of the bovine prolactin gene.

Nucleic Acids Res

August 1990

BioMolecular Research Department, W.R. Grace and Co-Conn., Washington Research Center, Columbia, MD 21044.

The 5'-flanking region of the bovine prolactin gene was cloned and sequenced. The expression of chimeric gene constructs containing 5'-flanking DNA fragments from the prolactin gene joined to a reporter gene encoding human growth hormone (hGH) was examined using transiently transfected rat pituitary cells. Prolactin nucleotide sequences located at position -1213 to -925 enhance the basal level of expression of growth hormone by 5-fold and function in a position- and orientation-independent fashion.

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Monoclonal antibody production in hollow fiber bioreactors using serum-free medium.

Biotechniques

February 1989

Washington Research Center, Dept. of Mammalian Cell Research, W.R. Grace and Co., Columbia, MD 21044.

Murine hybridoma cells that produce monoclonal antibody directed against human fibronectin have been cultured in VITAFIBER II and VITAFIBER V hollow fiber bioreactors using defined, serum-free WRC 935 medium. During a two-week growth period, following inoculation of the bioreactors, the cells proliferated to an extent where the bioreactor was filled with cultured cells. Using a 5 sq.

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The ammonium ion has been found to interfere in the Mohr method for the determination of chloride.

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