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D F Ward

Publications and source records attributed to D F Ward.

10 recordsLinked to original sources
PubMed1992

Effect of Escherichia coli nusG function on lambda N-mediated transcription antitermination.

The Escherichia coli Nus factors act in conjunction with the bacteriophage lambda N protein to suppress transcription termination on the lambda chromosome. NusA binds both N and RNA polymerase and may also interact with other Nus factors. To search for additional components of the N antitermination system, we isolated host revertants that restored N activity in nusA1 mutants. One revertant, nusG4, was mapped to the rif region of the E. coli chromosome and shown to represent a point mutation near the 3' end of the nusG gene. The nusG4 mutation also suppressed nusE71 but not nusASal, nusB5, nusC60 (rpoB60), or nusD026 (rho026). However, nusG+ expressed from a multicopy plasmid suppressed nusD026 and related rho mutants for both lambda and phage T4 growth. These results suggest that NusG may act as a component of the N antitermination complex. In addition, the data imply a role for NusG in Rho-dependent termination.

Bacterial Proteins↗
PubMed1990

CLONE 3: plasmid drawing and clone management software program for microcomputers.

CLONE 3 is a microcomputer software program which draws circular and linear plasmid maps, facilitates cloning operations and performs related sequence analysis and information retrieval functions. This article describes the use of the CLONE 3 program to streamline the flow of information in the research laboratory doing genetic engineering applications.

Base Sequence↗
PubMed1988

Unusual reaction to trifluoperazine.

A 19-year-old woman, recently discharged from the hospital and being treated for schizophrenia, presented with an unusual reaction to trifluoperazine. She complained of nausea and vomiting and experienced bilateral swelling of the tongue. Symptoms subsided when the medication was discontinued. Although dystonic reactions to high doses of phenothiazines are not uncommon, we postulate that this case represented an unusual allergic reaction to the medication.

Adult↗
PubMed1986

Plasmid map: a microcomputer program for display and storage of plasmid data.

We describe a plasmid map program which runs on an IBM PC microcomputer and facilitates the drawing of circular plasmid maps. The user enters information from the keyboard in the form of restriction enzyme sites, genes and their locations, and other plasmid markers such as promoters, origins, or other sites. This information can then be stored in a file for future reference. The plasmid map can be displayed on the screen, printed on a dot-matrix printer, or plotted on a Hewlett Packard HP7475A plotter.

Base Sequence↗
PubMed1986

A simple method for determination of red blood cell mechanical fragility in the rat.

A method for measuring the mechanical fragility of red blood cells suitable for use in small laboratory animals, such as rats, is reported because of lack of such data in the literature. Whole blood is mixed with phosphate buffered saline in a tube containing glass beads. The tubes are rocked for 90 minutes, centrifuged and the percent hemolysis determined. Varying the osmolality of the saline suspending medium had little effect on the mechanical fragility of rat red cells prior to the NaCl concentrations at which a significant change in osmotic hemolysis occurred. The duration of rocking increased the mechanical fragility. Varying the pH (6.4-8.0) had no effect. The size of the glass beads changed the mechanical fragility as did varying temperature. The mean mechanical fragility of rat red blood cells was 46% hemolysis (80 adult male animals). Because of the small volume of blood required with this method, mechanical fragility of red cells of other small laboratory animals also may be determined.

Animals↗
PubMed1976

Mutations in Escherichia coli that relieve catabolite repression of tryptophanase synthesis. Tryptophanase promoter-like mutations.

From a strain lacking adenyl cyclase and the catabolite-sensitive gene activator protein, two mutants were isolated that can synthesize tryptophanase. Each mutation is extremely closely linked to the tryptophanase structural gene. The mutations differ from one another in the rate of synthesis of tryptophanase that they permit in the genetic background in which they were isolated; they differ from one another and also from the wild type in the maximum rate of synthesis of tryptophanase that they permit in a genetic background with intact adenyl cyclase and catabolite-sensitive gene activator protein. Both mutations appear to lie in the tryptophanase promoter.

Chromosome Mapping↗