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Biomedical subjects

R C Hider

Publications and source records attributed to R C Hider.

At least 163 records · Page 9Linked to original sources
PubMed1980

Circular dichroism of elapidae protein toxins.

The effect of temperature variation on the circular dichroic spectra of four Elapid snake toxins (one short neurotoxin, two long neurotoxins and one cytotoxin) was determined and the results compared. The three neurotoxins have in common a delicately balanced conformation which can be perturbed independently of the predominant secondary structuring. Despite the many differences in sequence between long and short neurotoxins, the nature of this balance seems to be the same in both types and it is considered to involve an equilibrium between two defined conformers. Such properties could not be discerned in the cytotoxin studied, but related work suggests that they could nevertheless be present in some cases. In terms of global structure, long neurotoxins may have a greater proportion of 'random chain' inherent than short neurotoxins, the latter having extensive beta-sheet. The important feature of all toxins is deemed to be a conformational freedom defined by the secondary structuring and characteristic disulphide bridge formation. Possible relevance to toxicity of such a property is discussed.

Amino Acid Sequence↗
PubMed1979

The structure of melittin in lipid bilayer membranes.

0.15 M inorganic phosphate dramatically increased the alpha-helix content of melittin in aqueous solution. When melittin interacted with egg yolk phosphatidylcholine liposomes in the absence of inorganic phosphate, it was converted to an alpha-helix rich form, as postulated by Dawson et al. (Dawson, C.R., Drake, A.F. Helliwell, J. and Hider, R.C. (1978) Biochim. Biophys. Acta 510, 75--86).

Bee Venoms↗
PubMed1978

The effect of synthetic polymers on the electrical and permeability properties of lipid membranes.

1. The effect of two series of hydrophilic and hydrophobic polymers on the stability, conductivity and permeability towards water and leucine of black lipid membranes and liposomes is reported. 2. The changes in properties of these membrane preparations is related to bulk phase viscosity and dielectric measurements together with monolayer studies. 3. The hydrophobic polymers dramatically increase membrane stability, had no effect on conductivity, but increased the permeability coefficient of leucine. 4. The hydrophilic polymers produced minor, but significant changes to membrane properties. 5. It is concluded that not only basic polymers but also neutral and acidic macromolecules can interact strongly with lipid membranes.

Acrylic Resins↗
PubMed1978

The interaction of bee melittin with lipid bilayer membranes.

The influence of melittin and the related 8-26 peptide on the stability and electrical properties of bilayer lipid membranes is reported. Melittin, unlike the 8-26 peptide, has a dramatic influence on lipid membranes, causing rupture at dilute concentrations. The circular dichroism of melittin demonstrated that under physiological conditions, in water, melittin is in extended conformation, which is enhanced in aqueous ethanol. However in 'membrane-like' conditions it is essentially alpha-helical. Secondary structure predictions were used to locate possible alpha-helical nucleation centres and a model of melittin was built according to these predictions. It is postulated that melittin causes a wedge effect in membranes.

Bee Venoms↗
PubMed1971

Identification in skeletal muscle of a distinct extracellular pool of amino acids, and its role in protein synthesis.

1. The kinetics of radioactive labelling of extra- and intra-cellular amino acid pools and protein of the extensor digitorum longus muscle were studied after incubations with radioactive amino acids in vitro. 2. The results indicated that an extracellular pool could be defined, the contents of which were different from those of the incubation medium. 3. It was concluded that amino acids from the extracellular pool, as defined in this study, were incorporated directly into protein.

Amino Acids↗
PubMed1971

The effect of insulin on free amino acid pools and protein synthesis in rat skeletal muscle in vitro.

1. The effects of insulin in vitro on tissue pools and incorporation into protein of glycine and leucine in the extensor digitorum longus muscle of the rat are reported. 2. It was found that insulin decreased the lag period before the establishment of a linear rate of incorporation of radioactive glycine into protein. 3. The hormone increased the size of the free intracellular glycine pool. No such effect was found for leucine. The accumulation of radioactive glycine in the intracellular fluid compartment was increased. The content of radioactive leucine in the intracellular compartment was decreased. 4. Insulin decreased the specific radioactivity of both glycine and leucine in the extracellular fluid. 5. The hormone also decreased protein catabolism. 6. The effect on protein synthesis was not caused by an increase in the specific radioactivity of the extracellular pool but was possibly related to increased amino acid concentrations in this pool, which could in turn have affected the aggregation of ribosomes.

Amino Acids↗
PubMed1970

Permeability of the small intestine to substances of different molecular weight.

The permeability of the rabbit small intestine has been studied by measuring the plasma clearances of water-soluble molecules over the molecular weight range 60-33,000. An inverse relationship has been demonstrated between permeability and molecular weight. The significance of these findings in relation to current concepts of the ;pore hypotheses' is discussed, and the possible physiological and pathological implications are considered.

Animals↗
PubMed1969

Relationship between intracellular amino acids and protein synthesis in the extensor digitorum longus muscle of rats.

1. The incorporation into protein, and the accumulation into the free amino acid pools, of radioactive l-leucine and glycine was studied in rat extensor digitorum longus muscle. 2. The tissue was incubated first with (14)C-labelled and then with (3)H-labelled amino acid. 3. The experimental results were consistent with a model based on the premise that the amino acids in protein were incorporated directly from the extracellular pool.

Animals↗
PubMed1969

The sites of hydrolysis of dipeptides containing leucine and glycine by rat jejunum in vitro.

1. The effect of peptides containing leucine and glycine on accumulation of leucine and glycine by everted jejunal rings was studied. 2. It was shown that, on a molar basis, leucyl-leucine is a more effective inhibitor of uptake of [(14)C]leucine than is either leucylglycine or glycyl-leucine. These latter dipeptides behave alike. 3. The concentration of the dipeptides and their constituent amino acids in both the incubation medium and the tissue has been followed in these experiments by amino acid analysis. No leucine-containing peptides were observed in the tissue. 4. The inhibitory effects of the mixed dipeptides are altered by pH changes in an analogous way to the alterations in peptidase activity. 5. The experimental results indicate that leucine-containing peptides are hydrolysed before the transport step. 6. Glycylglycine, on the other hand, has only a small effect on the accumulation of glycine, although large amounts of the peptide accumulate unchanged in the tissue. This suggests that glycylglycine is taken up by a different mechanism to that for the leucine dipeptides.

Animals↗