PubMed Health⌕ Search

Biomedical subjects

D Ashford

Publications and source records attributed to D Ashford.

15 recordsLinked to original sources
PubMed2001

Effects of manipulating relative and absolute motion information during observational learning of an aiming task.

In the visual perception perspective of observational learning, the manipulation of relative and absolute motion information in visual demonstrations optimally directs learners' search towards appropriate task solutions. We assessed the effect of emphasizing transformational information and removal of structural information using point-light kinematic displays in approximating the model's relative motion patterns. Participants viewed computer-simulated point-light demonstrations or normal video demonstrations before and intermittently throughout 100 acquisition trials with knowledge of results on an underarm modified-dart aiming task. On the next day, all participants performed 20 retention trials without demonstrations. The kinematics of spatial and temporal coordination and control variables were examined relative to the model's action, as well as performance scores. The results indicated that approximation of the model's spatial and temporal coordination and control patterns was achieved after observation of either type of demonstrations. No differences were found in movement outcomes. In a second experiment, the effects of manipulating absolute motion information by slow-motion demonstrations were examined relative to real-time demonstrations. Real-time demonstrations led to a closer approximation to the model's spatial and temporal coordination patterns and better outcome scores, contradicting predictions that slow-motion displays convey intact relative motion information. We speculate that the effect of visual demonstration speed on action perception and reproduction is a function of task constraints--that is, novelty or familiarity of relative motion of demonstrated activities.

Adult↗
PubMed2000

An evaluation of process and outcomes from learning through reflective practice groups on a post-registration nursing course.

An evaluation of process and outcomes from learning through reflective practice groups on a post-registration nursing course Small groups were set up purposefully on a part-time post-registration Diploma in Professional Studies in Nursing programme to enable students to reflect on and learn from experience. The use of these groups was qualitatively evaluated by the use of in-depth interviews. Although there were many barriers to such learning, some students made significant developments in their critical thinking ability and underwent perspective transformations that led to changes in attitudes and behaviour. These are identified as an increased professionalism, greater autonomy in decision making, more self-confidence to challenge the status quo and make their own judgements, and a less rule-bound approach to their practice. The processes by which these changes occurred are identified as support and challenge within the groups offered by both the facilitators and other group members.

Attitude of Health Personnel↗
PubMed2000

Barriers to learning from reflection: a study of the use of groupwork with post-registration nurses.

There are few studies which describe the use of groups to facilitate reflection and even fewer which evaluate the effectiveness of such groups. Much of the literature discussing the techniques used to facilitate reflection suggests that learners willingly engage in such processes and find them enjoyable. This paper reports on a qualitative study of the use of groups to develop learning through reflection on a part-time post-registration diploma programme for nurses. The findings suggest that there are many barriers to learning which must be overcome before practitioners can use the opportunities to reflect on and learn from their experience. It is also contended that such learning may not necessarily be an enjoyable experience. The findings suggest that previous educational experience and the current culture in which nurses and midwives work, impose tremendous barriers to reflecting on, and learning from, experience. In particular these affect the willingness of learners to expose themselves to the judgement of others and their ability to be open to taking responsibility for their own learning. Other barriers to learning in groups are the effects of other group members, their commitment or resistance to shared learning, the ways in which group members interact with each other and facilitation styles.

Education, Nursing↗
PubMed1999

Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota).

A modified assay for inhibition of ice recrystallization which allows unequivocal identification of activity in plant extracts is described. Using this assay a novel, cold-induced, 36 kDa antifreeze protein has been isolated from the tap root of cold-acclimated carrot (Daucus carota) plants. This protein inhibits the recrystallization of ice and exhibits thermal-hysteresis activity. The polypeptide behaves as monomer in solution and is N-glycosylated. The corresponding gene is unique in the carrot genome and induced by cold. The antifreeze protein appears to be localized within the apoplast.

Antifreeze Proteins↗
PubMed1998

A carrot leucine-rich-repeat protein that inhibits ice recrystallization.

Many organisms adapted to live at subzero temperatures express antifreeze proteins that improve their tolerance to freezing. Although structurally diverse, all antifreeze proteins interact with ice surfaces, depress the freezing temperature of aqueous solutions, and inhibit ice crystal growth. A protein purified from carrot shares these functional features with antifreeze proteins of fish. Expression of the carrot complementary DNA in tobacco resulted in the accumulation of antifreeze activity in the apoplast of plants grown at greenhouse temperatures. The sequence of carrot antifreeze protein is similar to that of polygalacturonase inhibitor proteins and contains leucine-rich repeats.

Amino Acid Sequence↗
PubMed1997

Honeydew sugars and osmoregulation in the pea aphid Acyrthosiphon pisum

Pea aphids, Acyrthosiphon pisum, containing their symbiotic bacteria (untreated aphids) and experimentally deprived of their bacteria by treatment with the antibiotic rifampicin (antibiotic-treated aphids) were reared on the plant Vicia faba. The sugars in the honeydew produced by untreated aphids comprised predominantly the monosaccharides glucose and fructose, while the honeydew of antibiotic-treated aphids contained considerable amounts of oligosaccharides of up to 16 hexose units. The honeydew and haemolymph of the aphids were iso-osmotic, and their osmotic pressure was significantly lower in untreated aphids (0.91&shy;0.95 MPa) than in antibiotic-treated aphids (1.01&shy;1.05 MPa) (P<0.05). For insects reared on chemically defined diets containing 0.15&shy;1.0 mol l-1 sucrose (osmotic pressure 1.1&shy;4.0 MPa), the osmotic pressure of the aphid haemolymph did not vary with dietary osmotic pressure, but was regulated to approximately 1.0 MPa in untreated and 1.3 MPa in antibiotic-treated aphids. The sugars in the aphid honeydew varied with dietary sucrose concentration; with monosaccharides dominant at low concentrations and oligosaccharides dominant at high concentrations of dietary sucrose. The lowest dietary sucrose concentration at which honeydew oligosaccharides were detected was 0.2 mol l-1 for the antibiotic-treated aphids and 0.3 mol l-1 for untreated aphids. These data indicate that the aphid, and not its associated microbiota, mediates the synthesis of oligosaccharides when the osmotic pressure of the ingesta is high.

Journal Article↗
PubMed1995

Characterization of Neisseria elongata subsp. glycolytica isolates obtained from human wound specimens and blood cultures.

Four slightly yellow-pigmented, alpha-hemolytic, gram-negative coccobacilli, three from wound specimens and one from multiple blood cultures of a patient with endocarditis, were identified as Neisseria elongata subsp. glycolytica on the basis of their overall biochemical and genetic similarities to this subspecies. These strains resembled N. elongata in their guanine-plus-cytosine contents (55.6 to 57.1 mol%) and in their overall cellular fatty acid profiles, which are characterized by large amounts of 16:0, 16:1 omega 7c, and 18:1 omega 7c fatty acids. Their identities were confirmed by species-level DNA relatedness (hydroxyapatite method) to the type strains of all three N. elongata subspecies. The biochemical profiles and cultural characteristics of these strains resembled those of the type strain of N. elongata subsp. glycolytica except for the production of a weak yellow growth pigment and alpha-hemolysis on sheep blood agar. They differed from N elongata subsp. elongata by the production of catalase, by the production of alpha-hemolysis on sheep blood agar, and by acid production from D-glucose. They differed from N. elongata subsp. nitroreducens by the production of catalase and an inability to reduce nitrate. These studies suggest a pathogenic potential for N. elongata subsp. glycolytica, usually considered to be a transient colonizer in humans.

Bacterial Typing Techniques↗
PubMed1990

Two-domain structure of the native and reactive centre cleaved forms of C1 inhibitor of human complement by neutron scattering.

The C1 inhibitor component of human complement is a member of the serpin superfamily, and controls C1 activation. Carbohydrate analyses showed that there are seven O-linked oligosaccharides in C1 inhibitor. Together with six N-linked complex-type oligosaccharides, the carbohydrate content is therefore 26% by weight and the molecular weight (Mr) is calculated as 71,100. Neutron scattering gives an Mr of 76,000 (+/- 4000) and a matchpoint of 41.8 to 42.3% 2H2O, in agreement with this carbohydrate and amino acid composition. Guinier plots to determine the radius of gyration RG were biphasic. Neutron contrast variation of C1 inhibitor in H2O-2H2O mixtures gave an overall radius of gyration RG at infinite contrast of 4.85 nm, from analyses at low Q, and a cross-sectional RG of 1.43 nm. The reactive centre cleaved form of C1 inhibitor has the same Mr and structure as the native molecule. The length of C1 inhibitor, 16 to 19 nm, is far greater than that of the putative serpin domain. This is attributed to an elongated structure for the carbohydrate-rich 113-residue N-terminal domain. The radial inhomogeneity of scattering density, alpha, is large at 59 x 10(-5) from the RG data and 28 x 10(-5) from the cross-sectional analysis, and this is accounted for by the high oligosaccharide content of C1 inhibitor. The scattering data were modelled using small spheres. A two-domain structure of length 18 nm based on two distinct scattering densities accounted for all the contrast variation data. One domain is based on the crystal structure of alpha 1 antitrypsin (7 nm x 3 nm x 3 nm). The other corresponds to an extended heavily glycosylated N-terminal domain of length 15 nm, whose long axis is close to the longest axis of the serpin domain. Calculation of the sedimentation coefficient s0(20),w for C1 inhibitor using the hydrodynamic sphere approach showed that a two-domain head-and-tail structure with an Mr of 71,000 and longest axis of 16 to 19 nm successfully reproduced the s0(20),w of 3.7 S. Possible roles of the N-terminal domain in the function of C1 inhibitor are discussed.

Borohydrides↗
PubMed1987

The beta 1----2-D-xylose and alpha 1----3-L-fucose substituted N-linked oligosaccharides from Erythrina cristagalli lectin. Isolation, characterisation and comparison with other legume lectins.

The carbohydrate moieties of Erythrina cristagalli lectin were released as oligosaccharides by hydrazinolysis, followed by N-acetylation and reduction with NaB3H4. Fractionation of the tritium-labelled oligosaccharide mixture by Bio-Gel P-4 column chromatography and high-voltage borate electrophoresis revealed that it is composed of five neutral oligosaccharides. Structural studies by sequential exoglycosidase digestion in combination with methylation analysis and two-dimensional 1H-NMR showed that the major component was the fucose-containing heptasaccharide Man alpha 3(Man alpha 6)(Xyl beta 2)Man beta 4GlcNAc beta 4(Fuc alpha 3)GlcNAcol. This is the first report of such a structure in plant lectins. Small amounts of the corresponding afucosyl hexasaccharide were also identified, as well as three other minor components. The structure of the heptasaccharide shows the twin characteristics of a newly established family of N-linked glycans, found to date only in plants. The characteristics are substitution of the common pentasaccharide core [Man alpha 3(Man alpha 6)Man beta 4GlcNAc beta 4GlcNAc] by a D-xylose residue linked beta 1----2 to the beta-mannosyl residue and an L-fucose residue linked alpha 1----3 to the reducing terminal N-acetylglucosamine residue. The oligosaccharide heterogeneity pattern for Erythrina cristagalli lectin was also found for the lectins from four other Erythrina species and the lectins of two other legumes, Sophora japonica and Lonchocarpus capassa.

Carbohydrate Conformation↗
PubMed1986

Protein conformation of potato (Solanum tuberosum) lectin determined by circular dichroism.

The structure of potato (Solanum tuberosum) lectin, which is a hydroxyproline-rich glycoprotein, has been investigated by circular dichroism. The spectra of the native lectin, and of the oxidized, reduced and carboxymethylated and deglycosylated derivatives were examined, as was a hydroxyproline-rich glycopeptide and its deglycosylated derivative. It is concluded that the lectin contains about 35% polyproline II conformation, 34% type II beta-turn and 31% irregular conformation. No indications were found for the presence of alpha-helix or beta-sheet conformations. The polyproline II conformation is heat-stable, but is markedly destabilized by deglycosylation. The type II beta-turn is destabilized by cleavage of disulphide bonds.

Amino Acids↗
PubMed1982

The production and properties of an antiserum to potato (Solanum tuberosum) lectin.

Precipitation of potato (Solanum tuberosum) lectin by antisera was not affected by treatments that abolish lectin activity. An antiserum precipitated glycosylated derivatives of the lectin but not a deglycosylated peptide. The haemagglutination inhibition titre of this antiserum was not affected by removing anti-glycopeptide antibodies. This evidence suggests that the antiserum contains two populations of antibodies, specific for different domains of the lectin.

Animals↗
PubMed1982

Structural studies of the carbohydrate moieties of lectins from potato (Solanum tuberosum) tubers and thorn-apple (Datura stramonium) seeds.

1. Methylation analysis of potato (Solanum tuberosum) lectin and thorn-apple (Datura stramonium) lectin confirmed previous conclusions that both glycoproteins contained high proportions of l-arabinofuranosides and lesser amounts of d-galactopyranosides. The arabinofuranosides are present in both lectins as short unbranched chains containing 1-->2- and 1-->3-linkages, which are known to be linked to hydroxyproline. Galactopyranosides are present as monosaccharides, which are known to be attached to serine, in potato lectin and as both the monosaccharide and the 1-->3-linked disaccharide in Datura lectin. 2. Alkaline digestion of potato lectin and subsequent separation of the components by gel filtration led to the isolation of four fractions corresponding to the mono-, di-, tri- and tetra-arabinosides of hydroxyproline. The latter two fractions accounted for over 70% of the total hydroxyproline. 3. Methylation analysis was used to show that the triarabinoside contained only 1-->2-linkages between sugars, but that the tetra-arabinoside contained both 1-->2- and 1-->3-linkages. Direct-insertion mass spectrometry of these compounds using electron impact and chemical ionization, in a comparison with other known structural patterns, was used to determine the sequences of the sugars, which were Araf1-->2Araf1-->2Araf1-->Hyp and Araf1-->3Araf1-->2Araf1-->2Araf 1-->Hyp. 4. On the basis of optical rotation it had previously been suggested [Allen, Desai, Neuberger & Creeth (1978) Biochem. J.171, 665-674] that all the arabinose of potato lectin was present as the beta-l-furanoside. However, measurement of the optical rotations of the hydroxyprolyl arabinosides showed that whereas the diarabinoside had a molar rotation ([m]) value close to that predicted, the triarabinoside was more dextrorotatory and the tetra-arabinoside was less dextrorotatory than expected. Possible explanations for these findings are that, although the di- and tri-arabinosides contain exclusively beta-arabinofuranosides, in the tri-arabinoside, interactions between pentose units lead to an enhanced positive rotation. The tetra-arabinoside, however, is proposed to contain a single alpha-arabinofuranoside residue, which is responsible for the lower than expected positive rotation. The observed rotation of the tetra-arabinoside was found to be close to the theoretical value predicted on that basis. Furthermore, the action of a specific alpha-arabinofuranosidase on the tetrasaccharide was to remove a single arabinose residue, presumably the terminal non-reducing sugar, and to produce a product that was indistinguishable on electrophoresis from the triarabinoside. Changes in rotation were compatible with this assumption. 5. It is concluded that the structures of the hydroxyprolyl tri- and tetra-arabinosides of potato lectin are: betaAraf1-->2betaAraf1-->2betaAraf1-->Hyp and alphaAraf1-->3betaAraf1-->2betaAraf 1-->2betaAraf1-->Hyp. These are identical with compounds that have been isolated from the insoluble hydroxyproline-rich glycoproteins of plant cell walls.

Amino Acids↗
PubMed1981

Studies on the chemical modification and potato (Solanum tuberosum) lectin and its effect on haemagglutinating activity.

1. Modification of potato (Solanum tuberosum) lectin with acetic anhydride blocked 5.1 amino and 2.7 tyrosyl groups per molecule of lectin and decreased the haemagglutinating activity of the lectin. De-O-acetylation regenerated 2.0 of the tyrosyl groups and resulted in a recovery of activity. 2. Modification with citraconic anhydride or cyclohexane-1,2-dione did not greatly affect activity, although modification of amino and arginyl groups could be demonstrated. 3. Treatment with tetranitromethane nitrated 3.7 tyrosine residues per molecule of lectin with concomitant loss of activity. The presence of 0.1m-NN'N''-triacetylchitotriose (a potent inhibitor of the lectin) in the reaction medium protected all the tyrosyl residues from nitration and the lectin was fully active. 4. Modification of tryptophyl groups with 2-hydroxy-5-nitrobenzyl bromide and 2,3-dioxoindoline-5-sulphonic acid modified 0.9 and 2.6 residues per molecule of lectin respectively with a loss of activity in each case. Reaction of potato lectin with 2,3-dioxoindoline-5-sulphonic acid in the presence of inhibitor protected 2.4 residues of tryptophan from the reagent. Loss of haemagglutination activity was prevented under these conditions. 5. Reaction of carboxy groups, activated with carbodi-imide, with alpha-aminobutyric acid methyl ester led to the incorporation of 5.3 residues of the ester per molecule of lectin. Presence of inhibitor in this case, although protecting activity, did not prevent modification of carboxy groups; in fact an increase in the number of modified residues was seen. This effect could be imitated by performing the reaction in 8m-urea. In both cases the number of carboxy groups modified was close to the total number of free carboxy groups as determined by the method of Hoare & Koshland [(1967) J. Biol. Chem.242, 2447-2453]. Guanidination of lysine residues after carboxy-group modification gave less homoarginine than did the unmodified lectin under the same conditions, suggesting the formation of intramolecular cross-links during carbodi-imide activation. 6. It is suggested from the results presented that amino, arginyl, methionyl, histidyl and carboxyl groups are not involved in the activity of the lectin and that tyrosyl and tryptophyl groups are very closely involved. These findings are similar to those reported for other proteins that bind N-acetylglucosamine oligomers and also fit the general trend in other lectins.

Amino Acids↗
PubMed1977

Structural and composition of the N2 neuraminidase of influenza virus. Effect of carbohydrate content on the validity of molecular weight estimations.

Neuraminidase was isolated by proteolysis of the X7-(F1) (HON2) strain of influenza virus, and purified by gel filtration. The molecule contained a total of 46% (w/w) carbohydrate. The Mr was estimated as 152 500 (sedimentation diffusion) and 147 000 (sedimentation equilibrium). In 6 M guanidine-HCl the molecular weight was halved to 66 000 (sedimentation equilibrium). After irreversible reduction and blocking of sulphydryl groups the molecular weight was halved again to 33 500 (sedimentation equilibrium). These results confirm the tetrameric model of neuraminidase structure. They also provide strong evidence that the tetramer is composed of two disulphide linked dimers, themselves associated by non-covalent linkages. Theoretical considerations based on this model predict that assembly of the molecule must be accompanied by allosteric conformational changes in the subunits. The high carbohydrate content was thought to explain the discrepancy between the molecular weight values for the neuraminidase polypeptide obtained by different methods, and also the exceptional resistance of the molecule to digestion by proteolytic enzymes.

Amino Acids↗