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Biomedical subjects

A E Russell

Publications and source records attributed to A E Russell.

35 records · Page 2Linked to original sources
PubMed1974

Differential anion effects on thermal stability of collagen in the dispersed and aggregated states.

The effects of KCNS and KI on thermal transition temperatures of calf skin collagen molecules in dilute acid solution and precipitated collagen fibrils from the same source were compared as a function of salt concentration and pH. The two salts produced qualitatively similar effects on each collagen form, but the response shown by single collagen molecules in dilute solution differed from that observed for molecular aggregates present in native-type fibrils.

Animals↗
PubMed1974

Effect of pH on thermal stability of collagen in the dispersed and aggregated states.

Thermal stabilities of mature insoluble collagen, salt-precipitated fibrils of acid-soluble collagen and acid-soluble collagen in solution were compared as a function of acid pH. Both insoluble and precipitated collagens showed large parallel destabilization with decrease in pH, whereas the intrinsic stability of individual collagen molecules in dilute solution was comparatively unaffected.

Animals↗
PubMed1973

Effect of alcohols and neutral salt on the thermal stability of soluble and precipitated acid-soluble collagen.

The effects of mono- and poly-hydric alcohols in the presence of KCl on the intrinsic stability of collagen molecules in dilute acid solution were compared with corresponding solvent and salt effects on the increased stability of the aggregated molecules in salt-precipitated fibrils. Salt addition decreased solubility and increased the thermal stability of fibrils, but progressively decreased the stability of collagen molecules in solution. In contrast, the alcohols enhanced solubility and decreased fibril stability, the effects increasing with solvent hydrocarbon chain length and with decreasing hydroxyl/methylene-group ratio. Molar destabilization of dissolved collagen by alcohols was lower than for fibrils, and at low salt concentration, both ethylene glycol and glycerol were structural stabilizers. Electron-micrograph studies indicated that salt-precipitated fibrils tended to adopt the native aggregation mode, and qualitatively similar solvent effects were observed in insoluble collagens. Implications of the experimental findings are discussed in terms of a model in which electrostatic and apolar interactions mainly govern the excess of stability in collagen fibrils whereas intrinsic stability of single molecules is a function of polar interactions and polypeptide-chain rigidity.

1-Propanol↗
PubMed1972

Effect of compounds of the urea-guanidinium class on renaturation and thermal stability of acid-soluble collagen.

The effects of guanidinium salts in decreasing the renaturation rate and lowering the thermal stability of acid-soluble calf-skin collagen have been compared with those of formamide and urea. With the exception of guanidinium sulphate at higher concentrations, no qualitative differences were apparent in the effects of these perturbants, which thus differed only in molar activity. Activity variation in the guanidinium salts reflected a net effect resulting from additivity of cation and anion contributions. As observed in other protein systems, lyotropic activity increased in the series formamide<urea<guanidinium ion, and in the guanidinium salts in the anion order fluoride<sulphate<chloride<bromide<nitrate<iodide. Low activities of guanidinium fluoride and sulphate were attributable to counter-effects of the anions, which acted as structural stabilizers. Changes in renaturation kinetics induced by either temperature or added perturbants appeared to conform with the Flory-Weaver model for the collagen transition. Additivity and non-specificity of the observed effects are discussed with particular reference to a common mechanism involving weak, non-saturated binding of perturbants at protein peptide groups.

Animals↗
PubMed1971

The effects of certain glycols, substituted glycols and related organic solvents on the thermal stability of soluble collagen.

The effects of a number of related diols, substituted diols and glycerol on the thermal stability of acid-soluble calf skin collagen were investigated. Thermal transition temperatures were determined by optical rotation measurement. Short-chain diols with terminal hydroxyl groups, i.e. ethylene glycol and propane-1,3-diol, stabilized the protein at all accessible concentrations. Stabilization was also observed with glycerol and diethylene glycol. Higher homologues in the diol series produced various effects, as did hydroxyl-group positional isomerism. Monoalkyl substitution of diols progressively lowered the denaturation temperature of collagen. Results are discussed in relation to possible mechanisms of perturbant action.

Animals↗
PubMed1971

The effects of glycols on the renaturation of soluble collagen.

The effects of a number of related glycols and substituted glycols on the renaturation kinetics of acid-soluble calf-skin collagen have been investigated. Optical rotation recovery was monitored at a fixed temperature in the presence of perturbants and the initial rates of reaction were determined. The effects of perturbants on stability of the native protein are compared with their action in the renaturing systems. The relationship between initial recovery rates and fixed-time [alpha]-values is shown to be dependent upon the renaturation temperature. The influence of perturbant concentration on recovery rates is discussed in terms of present theories of the mechanism of collagen renaturation.

Animals↗
PubMed1969

The decomposition of soluble collagen by gamma-irradiation.

1. The effect of gamma-irradiation in the range 1 krad-10 Mrads on freeze-dried acid-soluble collagen was studied. 2. The specific-rotation and reduced-viscosity recoveries after heating and cooling of the irradiated collagen in solution showed a high degree of dependence on irradiation dose, with reduced viscosity showing significantly less recovery than specific rotation on increasing the irradiation dose. 3. The dependence of reduced viscosity on concentration was greatly decreased with increased doses of gamma-irradiation. 4. The melting temperature measured by optical rotation also decreased as the irradiation dose was increased, and at low doses was distinctly biphasic. 5. Physical properties showed that the action of gamma-irradiation up to 10 Mrads occurred in two distinct phases, with the early changes being extremely sensitive to irradiation dose. 6. The action of the gamma-irradiation is discussed in terms of the structure of tropocollagen.

Collagen↗