Registered nurses' perceptions of liberal education.

Educators in higher education and nursing stress the importance of liberal education in helping professionals address the complexity, ambiguity, and rapid change inherent in current practice. Yet, little is known about nurses' perceptions and use of liberal education either personally or professionally. This article explores RNs' perceptions of liberal education, including its personal and professional impact and its acquisition. Based on interviews with 17 practicing nurses, important themes about liberal education were derived using phenomenological analysis. The findings suggest issues that educators might examine to improve the acquisition of liberal education and its integration with professional practice.

The influence of liberal education on professional nursing practice: a proposed model.

Nursing has embraced philosophically the importance of liberal education to professional practice. Yet there has been little exploration of how and if liberal education influences professional action. Based on a series of studies designed to examine the role of liberal education in professional practice, this article describes six competencies related to liberal and professional education and puts forth a model of practice that appears to be influenced by liberal education.

Sequence analysis of bovine lens aldose reductase.

The covalent structure of bovine lens aldose reductase (alditol-NADP+ oxidoreductase, EC 1.1.1.21) was determined by sequence analysis of peptides generated by specific and chemical cleavage of the homogeneous apoenzyme. Peptides, purified by reverse-phase high performance liquid chromatography were subjected to compositional analysis and sequencing by gas-phase automated Edman degradation. Aldose reductase was found to contain 315 amino acid residues. The enzyme is blocked at the amino terminus, and mass spectrometry was employed to identify the blocking acetyl group and to sequence the amino-terminal tryptic peptide. The aldose reductase was shown to contain no carbohydrate despite the fact that the enzyme contains the consensus sequence -Asn-Lys-Thr- for N-linked glycosylation. Comparative sequence analysis and application of algorithms for prediction of secondary structure and nucleotide binding domains are consistent with the view that aldose reductase is a double-domain protein with a beta-alpha-beta secondary structural organization. The NADPH binding site appears to be associated with the amino-terminal half of the enzyme. Modeling studies based on the tertiary structures of dihydrofolate and glutathione reductases indicate that the NADPH binding site begins at Lys-11 and continues with a beta-alpha-beta fold characteristic of nucleotide binding proteins.

A new tool for peptide separation.

A family of reagents has been developed (Pep-Seps) which provide separations of peptides based upon the presence or absence of a single type of amino acid. This separation is achieved through a reversible, covalent attachment of the peptide to the Pep-Seps reagents. Pep-Seps provide a more specific separation than most forms of HPLC and may be used to complement HPLC in peptide separations and isolations. Several specific applications will be discussed.

Presence of proteins and glutamate as major constituents of the venom of the spider Araneus gemma.

The venom from the spider Araneus gemma contains an inhibitor of physiologic glutamate receptors and of glutamate binding sites in brain synaptic membranes. In the present study the chemical composition of the venom was examined in order to determine the presence of constituents that may have physiologically important actions on the prey. The milked venom contains high concentrations of protein (approximately equal to 200 micrograms/microliter) and of glutamate (130-425 mM) and very low concentrations of epinephrine, epinine, dopamine and 3,4-dihydroxyphenylacetic acid. There is also marked heterogeneity in the venom peptides detected by SDS gel electrophoresis. The presence of free glutamate may be very important for the actions of the glutamate receptor inhibitor in the venom.

Spider venoms inhibit L-glutamate binding to brain synaptic membrane receptors.

The venoms from three spider species, Araneus gemma, Neoscona arabesca, and Argiope aurantia, were shown to inhibit the high-affinity, sodium-independent L-glutamate-binding sites in rat brain synaptic membranes. The same three venoms caused concentration-dependent inhibition of the activity of the glutamate-binding glycoprotein purified from rat brain synaptic membranes. The venom milked from the glands of Araneus gemma was the most active inhibitor of L-glutamate binding, causing 60-80% inhibition of both synaptic membrane and purified protein binding activity at 0.01 unit. The inhibitory activity of this venom was associated with a single protein peak obtained from gel permeation chromatography of the venom. Finally, the effect of the venom from Araneus gemma on the synaptic membrane glutamate-binding sites was slowly reversible. These observations indicate that the spider venoms have a direct effect on the recognition sites for L-glutamic acid in brain synaptic membranes and that these sites are related to the physiologic glutamate receptors.