A survey of research-related activities and perceived barriers to research utilization among professional oncology nurses.

PURPOSE/OBJECTIVES: To identify nursing staff members' current research-related activities, knowledge of research utilization, and perceived barriers to using research in practice. DESIGN: Descriptive, cross-sectional survey design with self-report questionnaires. SETTING: National Cancer Institute-designated comprehensive cancer center located in a mid-Atlantic metropolitan area. SAMPLE: Convenience sample of 82 registered nurses employed in the cancer center who completed and returned the questionnaire; the majority had baccalaureate degrees or higher, were an average of 33 years old, were nurses for a mean of 8.8 years, and worked at the center a mean of 5.6 years. METHODS: Four-part, 38-item, self-report questionnaires were distributed to nursing staff and a leadership group by members of the departmental Nursing Research Committee; respondents returned completed questionnaires to designated locations in the center. MAIN OUTCOME MEASURES: Knowledge and attitudes about research utilization, perceived barriers to using research in practice, and current research-related activities. FINDINGS: Most respondents were familiar with the concept of research utilization and found research to be of value to their practice. They cited a number of barriers to using research findings and reported little participation in research-related activities. Advanced clinical practitioners with master's degrees tended to participate more frequently in research-related activities. CONCLUSIONS: Although nurses appeared to be aware of research utilization and value it, they perceived barriers to using research findings in practice and did not routinely participate in research-related activities. The findings support other research in this area and reveal educational needs. IMPLICATIONS FOR NURSING PRACTICE: The findings provided baseline information for a departmental research utilization program and suggested strategies and activities that could be incorporated into the program.

Properties of an Escherichia coli mutant deficient in phosphoenolpyruvate carboxylase catalytic activity.

A mutant Escherichia coli (Ppcc-) which was unable to grow on glucose as a sole carbon source was isolated. This mutant had very low levels of phosphoenolpyruvate carboxylase activity (approximately 5% of the wild type). Goat immunoglobulin G prepared against wild-type phosphoenolypyruvate carboxylase cross-reacted with the Ppcc- enzyme. The amount of enzyme protein in the mutant cells was similar to that found in wild-type cells, but it had greatly diminished specific activity. The catalytically less active mutant enzyme retained the ability to interact with fructose 1,6-bisphosphate, but did not exhibit stabilization of the tetrameric form by aspartate. The pI of the mutant protein was lower (4.9) than that of the wild-type protein (5.1). After electrophoresis and immunoblotting of the partially purified protein, several immunostaining bands were seen in addition to the main enzyme band. A novel method for showing that these bands represented proteolytic fragments of phosphoenolpyruvate carboxylase was developed.

Escherichia coli phosphoenolpyruvate carboxylase. Studies on the mechanism of synergistic activation by nucleotides.

Kinetic studies were done to obtain a quantitative estimation of the synergistic interactions that occur between phosphoenolpyruvate carboxylase (orthophosphate:oxaloacetate carboxylase (phosphorylating) E.C. 4.1.1.31) from Escherichia coli K12 and various combinations of its primary substrate, P-enolpyruvate, and the activators acetylcoenzyme A, CDP, GTP, and fructose 1,6-bisphosphate. The analysis involves the evaluation of apparent K values, KS for P-enolpyru;ate and KA for activators, as a function of the concentration of P-enolpyruvate or another activator in the case of KA determinations. Methods are presented which allow the determination of dissociation constants for P-enolpyruvate and activators from binary, ternary, and quaternary complexes of enzyme with substrates or activators, or both. It was observed that synergistic activation occurs with acetyl coenzyme A and all of the coactivators but not with fructose 1,6-bisphosphate and the other co-activators. The enhancement of binding from the binary enzyme substrate (or activator) complex to the ternary or quaternary complexes is in the range of 100-fold. The dissociation constants for P-enolpyruvate, acetyl coenzyme A, CDP, and fructose 1,6-bisphosphate are the same from any active enzyme species. Synergistic activation by multiple activators reflects the ability of co-activators to shift the equilibrium concentrations of active enzyme species away from the inactive forms via a modified "cascade" scheme, thus decreasing the probability that dissociation of any one activator will yield an inactive enzyme species.

Chromatographic evidence for the existence of another species of luteinizing hormone-releasing factor (LRF).

Fractionation of ultrafiltrates of rat hypothalamic extracts has been performed on Sephadex LH-20 in dimethylformamide/water. The fractions were examined for their content of luteinizing hormone-releasing activity by bioassay in vitro utilizing LH radioimmunoassay, and also for their content of LRF decapeptide-like material by direct radioimmunoassay. Each method revealed the same pattern of activity. This consisted of a major peak whose elution position coincided with that of authentic decapeptide, and a minor region which closely preceded it, often taking the form of a shoulder on the leading edge of the main peak. The active component in the minor peak could be completely resolved by repeated filtration in the same system thus indicating that it represented another gonadotropin-releasing species rather than a chromatographic artefact although its biological and immunological activities indicate that its structure must resemble closely that of the decapeptide.