Suspension In Presence Research Articles

Study of the degradation of flocculants—Copolymers of acrylamide with potassium- p-styrene sulphonate in aqueous solution under the influence of K 2S 2O 8

The degradation patterns of statistical acrylamide copolymers with the potassium salt of p-styrene sulphonic acid in 0·4% aqueous solutions under the influence of K 2S 2O 8 at 50°C have been studied. The possibility of effectively regulating the molecular masses of the copolymers by changing the concentration of K 2S 2O 8, temperature and the duration of degradation has been demonstrated. From the kinetic data of degradation the authors evaluate the polydispersity by molecular mass of the initial copolymer samples and estimate the sedimentation indices of an ochre suspension in presence of copolymers as a function of their concentration, molecular mass and chemical composition.

Polyacrylamide-sodium kaolinite interactions: Flocculation behavior of polymer clay suspensions

The behavior of Na-kaolinite suspensions in presence of high-molecular-weight polyacrylamide is investigated experimentally. In analyzing the effect of polymer, three different domains are found: at low concentrations the polymer acts as a stabilizer, at intermediate concentrations enhanced flocculation is observed, and at high concentration the suspension is again stabilized. The mechanism of polymer action is analyzed in the light of adsorption data obtained using radiolabeled polymer. A correlation is established between adsorption strength and the mode of particles association in the three domains. The nature of the adsorption forces is discussed in terms of the surface chemistry of Na-kaolinite.

Resistance of Human Erythrocytes Containing Elevated Levels of Vitamin E to Radiation-Induced Hemolysis

Human erythrocytes were isolated from the blood of healthy donors and then incubated in the presence of suspensions of alpha-tocopherol for 30 min at 37 degrees C. Unabsorbed tocopherol was removed by centrifugation using several washes of isotonic phosphate-buffered saline. Washed erythrocytes were resuspended to 0.05%. Hct and exposed to hemolyzing doses of 60Co gamma radiation, and hemolysis was monitored continuously by light scattering at 700 nm in a recording spectrophotometer. The extent of hemolysis with time was sigmoid and data analysis was carried out on the time taken for 50% hemolysis to occur (t50%). The vitamin E content of erythrocytes was significantly elevated by the incubation procedure and resulted in the cells exhibiting a significantly increased resistance to hemolysis as reflected by the extended t50% values. Oral supplementation of 500 IU of vitamin E per day to eight normal human subjects for a period of 16 days also resulted in their washed erythrocytes exhibiting a significant increase in resistance to radiation-induced hemolysis. When comparing vitamin E incubated cells with control cells, both the dose-reducing factor (DRF) and the time for 50% hemolysis quotient (Qt50%) were observed to increase with increasing radiation dose.

Studies on the Flow and Sedimentation Characteristics of Sodium Bentonite Suspensions in Presence of Electrolytes and Humic Acids

Studies on the Flow and Sedimentation Characteristics of Sodium Bentonite Suspensions in Presence of Electrolytes and Humic Acids

Flow Behaviour of Bentonite Suspensions in Presence of Electrolytes

Flow Behaviour of Bentonite Suspensions in Presence of Electrolytes

Phospholipase A 2 from sheep erythrocyte membrane CA 2+ dependence and localization

The calcium dependence and the time course of phosphatidylethanolamine and phosphatidylcholine degradation by sheep erythrocyte membrane suspensions in presence of Triton X-100 were investigated. One enzyme with phospholipase A 2 specificity was found to be responsible for both phosphatidylethanolamine and phosphatidylcholine degradation. The localization of this enzyme in the membrane of the sheep erythrocyte was investigated by proteolytic treatment of sealed erythrocyte ghosts from the outside and of ghosts which had both sides of the membrane exposed to chymotrypsin. The inability of sealed ghosts to take up chymotrypsin was followed by flux measurements of [ 14C]dextran carboxyl previously trapped in the ghosts. No efflux of the marker was found during the proteolytic treatment. By comparing the residual phospholipase activities in the membranes from both ghost preparations, we concluded that the phospholipase is oriented to the exterior of the sheep erythrocyte.

EFFECTS OF DIHYDROSTREPTOMYCIN ON AMINO ACID INCORPORATION INTO THE PROTEINS OF M. TUBERCULOSIS (BCG)

A study has been made of the effects of dihydrostreptomycin on amino acid incorporation into the proteins of M. tuberculosis (BCG). Suspensions of this organism on incubation at 37° with glycine-1-C14give rise, aerobically, to labelled proteins in which 80% of the radioactivity appears in the glycine and serine moieties of the proteins and about 20% in alanine and aspartic acid. In presence of glycine-2-C14, radioactivity appears in a larger number of amino acids of the protein. Incubation with serine-3-C14leads to a distribution of radioactivity in the amino acids in BCG proteins but alanine-1-C14and valine-1-C14give rise to proteins with the radioactivity almost entirely in the corresponding amino acids. The process of aerobic incorporation of radioactivity from glycine-1-C14in BCG proteins is stimulated by the presence of glucose, glycerol, sodium pyruvate, sodium stearate, or sodium benzoate in the medium in which the cells are incubated, the rate of incorporation being approximately constant over a period of 4 hours. The incorporation depends largely on the presence of oxygen. Dihydrostreptomycin (33 μg per ml) markedly inhibits labelling of proteins in the cell suspensions in presence of radioactive amino acids, the inhibition increasing with concentration of the streptomycin to an optimal concentration of 200 μg/ml. Penicillin and isonicotinic hydrazide are inactive but chloromycetin is an effective inhibitor. Cyanide, arsenite, and azide are inhibitory. The presence of lecithin stimulates incorporation of radioactivity from glycine-1-C14into BCG proteins. Dihydrostreptomycin inhibitions of amino acid incorporation into BCG proteins increase with time of incubation of the cells with the drug. Concentrations of dihydrostreptomycin that inhibit labelled amino acid incorporation into labelled proteins by 50% have no effect on BCG respiration. The drug has no inhibitory effect on labelled amino acid incorporation in E. coli or Ehrlich ascites carcinoma cells in vitro but is effective with M. phlei. It does not affect selectively the distribution of radioactivities of the component amino acids of BCG proteins; only the total radioactivity incorporated into the proteins is diminished. The results lead to the conclusion that dihydrostreptomycin brings about an inhibition of protein synthesis in the BCG strain of M. tuberculosis at concentrations at which it exerts antibiotic effects.

EFFECTS OF DIHYDROSTREPTOMYCIN ON AMINO ACID INCORPORATION INTO THE PROTEINS OF M. TUBERCULOSIS (BCG)

A study has been made of the effects of dihydrostreptomycin on amino acid incorporation into the proteins of M. tuberculosis (BCG). Suspensions of this organism on incubation at 37° with glycine-1-C14give rise, aerobically, to labelled proteins in which 80% of the radioactivity appears in the glycine and serine moieties of the proteins and about 20% in alanine and aspartic acid. In presence of glycine-2-C14, radioactivity appears in a larger number of amino acids of the protein. Incubation with serine-3-C14leads to a distribution of radioactivity in the amino acids in BCG proteins but alanine-1-C14and valine-1-C14give rise to proteins with the radioactivity almost entirely in the corresponding amino acids. The process of aerobic incorporation of radioactivity from glycine-1-C14in BCG proteins is stimulated by the presence of glucose, glycerol, sodium pyruvate, sodium stearate, or sodium benzoate in the medium in which the cells are incubated, the rate of incorporation being approximately constant over a period of 4 hours. The incorporation depends largely on the presence of oxygen. Dihydrostreptomycin (33 μg per ml) markedly inhibits labelling of proteins in the cell suspensions in presence of radioactive amino acids, the inhibition increasing with concentration of the streptomycin to an optimal concentration of 200 μg/ml. Penicillin and isonicotinic hydrazide are inactive but chloromycetin is an effective inhibitor. Cyanide, arsenite, and azide are inhibitory. The presence of lecithin stimulates incorporation of radioactivity from glycine-1-C14into BCG proteins. Dihydrostreptomycin inhibitions of amino acid incorporation into BCG proteins increase with time of incubation of the cells with the drug. Concentrations of dihydrostreptomycin that inhibit labelled amino acid incorporation into labelled proteins by 50% have no effect on BCG respiration. The drug has no inhibitory effect on labelled amino acid incorporation in E. coli or Ehrlich ascites carcinoma cells in vitro but is effective with M. phlei. It does not affect selectively the distribution of radioactivities of the component amino acids of BCG proteins; only the total radioactivity incorporated into the proteins is diminished. The results lead to the conclusion that dihydrostreptomycin brings about an inhibition of protein synthesis in the BCG strain of M. tuberculosis at concentrations at which it exerts antibiotic effects.

VIII.—The Stability of Suspensions. I. The Rate of Sedimentation of Kaolin Suspensions by Salts at Varying Hydrogen Ion Concentrations

Summary1. The rates of sedimentation of a kaolin suspension in presence of varying concentrations of a salt (sodium chloride, potassium chloride, sodium sulphate, di-sodium hydrogen phosphate, sodium citrate, calcium chloride, calcium sulphate, monocalcium phosphate, “superphosphate”, aluminium chloride, ferric chloride or lanthanum chloride) have been compared at various pH values. Abnormal results are obtained with sodium chloride, monocalcium phosphate, aluminium, ferric and lanthanum chlorides.2. Sodium chloride increases the rate of sedimentation in alkaline solution, but actually inhibits it in acid solution.3. In concentrations of monocalcium phosphate above 0·06 per cent, abnormal sedimentation in alkaline solution takes place, with the result that it is much more complete than at the corresponding concentrations in acid solution.4. In acid solution the tervalent ions, aluminium, ferric and lanthanum have little effect, but a zone of very marked flocculation occurs at pH 7–8. This zone separates a region within which the unsedimented particles are negatively charged from a region within which they are positively charged.