The mechanism of repeated precipitation on dislocations

1973 ◽  
Vol 7 (9) ◽  
pp. ix
Author(s):  
E. Nes
2021 ◽  
Vol 1045 ◽  
pp. 32-39
Author(s):  
Nikolai Shapkin ◽  
Natalia Maslova ◽  
Evgeniy Papynov ◽  
Vladimir Kaminskii ◽  
Alevtina Kapustina ◽  
...  

The interaction of magnesium carbonate with polyphenylsiloxane under the conditions of mechanochemical activation with subsequent heating has been investigated. Based on the TGA and DTA data, it has been shown that, upon heating up to 420°C, the reaction proceeded completely with the release of carbon dioxide. The polymer was dissolved in DMFA and purified by repeated precipitation with water. The polymer yield was 64%. The residue insoluble in organic solvents has been obtained by evaporation of an aqueous solution. The composition and structure of the synthesis products have been analyzed by means of element analysis, IR spectroscopy, and diffractometry. It has been demonstrated that the fraction soluble in DMFA had a silicon-to-magnesium ratio equal to 4.2, while the fraction isolated from water had this ratio equal to 1.0. The IR and XRD data enabled one to conclude that, regardless of the different compositions, the structures of all fractions were similar and corresponded to mesomorphic layered polymers produced by the ion exchange method.


Tobacco mosaic was the first disease shown to be caused by a filter-passing virus, and Beijerinck (1898) suggested as its cause a “contagium vivum fluidum", Since then many other theories have been advanced, but there has been little positive evidence to indicate whether the virus more nearly resembled organisms such as small bacteria or chemical molecules such as the larger proteins. Recently, however, Stanley has isolated from tobacco (1936a) and tomato (Stanley and Loring 1936) plants suffering from mosaic a protein which he describes as crystalline and as possessing the properties of the virus. When susceptible plants were inoculated with this protein at a dilution of 10 -9 they developed typical symptoms of the disease. The protein was obtained from infective sap by repeated precipitation with 40% saturated ammonium sulphate solution, and by adsorption on and washing from celite. The “crystals” described by Stanley were small needles produced by precipitation with acid ammonium sulphate. A number of statements in Stanley’s earlier paper (1935 more especially those dealing with the nitrogen content and the serological activity, made us doubt the purity of his product, and preliminary experiments with methods similar to those used for the preparation of suspensions of potato virus “X” (Bawden and Pirie 1936) gave us products with much higher precipitation end-points with antisera than those claimed by Stanley. We have now exchanged material with Dr. Stanley and find no gross differences in the activities of our respective products. We have found, however, that by further purification the protein in neutral solution can be obtained in liquid crystalline states. Also, as will be shown later, there are considerable differences in the chemical descriptions given of the virus protein; some of these differences have already been resolved, and others presumably will be by future work.


1976 ◽  
Vol 192 (1109) ◽  
pp. 439-449 ◽  

Rabbit myosin prepared in the conventional manner by repeated precipitation at low ionic strength was recently shown to contain substantial amounts of impurities; the principal impurity is a component of the myofibril called C-protein. Because antiserum to such conventionally prepared myosin has been used in the past for labelling studies of muscle, it was necessary to study the immunological characteristics of myosin and C-protein and in particular to test the specificity of this antiserum. Antisera to both rabbit myosin and C-protein have been successfully elicited in goats. These antisera have been analysed by immunodiffusion and by precipitin reactions in solution. The analysis has been helped by the examination of immunoprecipitates by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulphate. It is concluded that: ( a ) C-protein and myosin are antigenically distinct and therefore that C-protein is not derived from myosin. ( b ) Purified myosin can behave as a classically simple antigen giving a single precipitin line when diffused against its homologous antiserum. ( c ) C-protein is a powerful immunogen; the amount present as an impurity in myosin prepared in the conventional way by repeated precipitation at low ionic strength is capable of eliciting a large amount of antibody. Consequently the pattern obtained by labelling myofibrils with antiserum to conventionally prepared myosin would contain information about the location of C-protein superimposed on information about the location of myosin.


1937 ◽  
Vol 65 (1) ◽  
pp. 75-89 ◽  
Author(s):  
Theodore J. Abernethy

The capacity of the serum of rabbits following intradermal pneumococcus infections to precipitate in the presence of pneumococcus C polysaccharide has been studied during the resultant periods of active infection and during recovery. In rabbits infected with Type I, III, or VIII pneumococci, large hemorrhagic lesions are produced which frequently bring about death of the animals after a febrile illness of 3 to 4 days. Repeated precipitation tests with the sera of these animals have been uniformly and consistently negative, not only during the acute illness but in the recovery period as well. On the other hand, the sera of monkeys of the Macacus cynomolgos species actively ill with experimental Type III pneumonia have been shown to react in precipitation tests with the C substance. The serum reaction appears within the first 24 hours after infection, remains positive in high titer for 2 to 3 days during the acute illness, and disappears with the onset of recovery. The precipitation reaction with C also occurs with the sera of monkeys following intradermal and intraperitoneal infection with pneumococci. The results of precipitation tests of the serum of monkeys during experimental pneumonia are similar to those obtained with the sera of patients suffering from pneumococcus lobar pneumonia. From the results of these studies it would appear improbable that the demonstration of the serum precipitation phenomenon with C polysaccharide in monkeys, and possibly also in man, is conditioned by previous exposure to pneumococcus antigen.


1966 ◽  
Vol 12 (2) ◽  
pp. 313-321 ◽  
Author(s):  
K. Matsushima ◽  
F. J. Simpson

Aerobacter aerngenes produces an inducible D-allose 6-phosphate ketol isomerase that nonspecilically isomerizes ribose 5-phosphate. The isomerase was separated from other isomerases present in extracts of cells grown on D-allose by repeated precipitation with protamine. Eighty percent of the activity of the purified preparation was lost on storage at 0 °C for 48 hours. The enzyme was most active and most stable at pH 8.5 and most active at 40 °C. Cobalt, manganese, magnesium, and phosphate ions inhibited at 0.05 M. Mercuric chloride, p-chloromer-curiphenylsulfonate, and iodoacetate also inhibited the isomerase but this was prevented by the addition of cysteine or reduced glutathione. These thiols also reactivated the enzyme when activity was lost during dialysis. 6-Phosphoallonate was a strong inhibitor and to a lesser degree 6-phosphogluconate, 6-phosphoglucosamine, 5-phosphoribonate, and erythrose 4-phosphate. For allose 6-phosphate Ks was 1.2 × 10−3 M and for ribose 5-phosphate, 4.5 × 10−3 M.


1952 ◽  
Vol 30 (6) ◽  
pp. 685-692 ◽  
Author(s):  
L. R. Wetter

A protease concentrate was obtained from the culture medium of Mortierella renispora Dixon-Stewart (PRL 26) by repeated precipitation with ammonium sulphate. The specific activity of the mold protease compared favorably with that of crystalline trypsin. The pH optimum was broad, with a maximum at a pH of 7.5 when hemoglobin was used as the substrate. A study of the pH stability characteristics showed that it was stable over a wide range (4.9 to 9.5) at 1 °C. and 25 °C. Ferrous ions caused a considerable increase in the activity of the enzyme preparations, other metals were ineffective as activators.


1970 ◽  
Vol 48 (3) ◽  
pp. 645-651 ◽  
Author(s):  
John C. Sutton ◽  
Paul H. Williams

The extracellular polysaccharide fraction of Xanthomonas campestris was precipitated with hexadecyltrimethylammonium bromide from aqueous extracts of cabbage leaves infected with the black rot pathogen, and further purified by repeated precipitation with ethanol. The polysaccharide fraction was shown to be similar to extracellular polysaccharide fraction purified from culture fitlrates of X. campestris. Sugars present in samples of acid-hydrolyzed polysaccharide were identified by gas–liquid chromatography. Chromatograms showed that polysaccharide purified from infected cabbage leaves contained glucose, mannose, and glucuronolactone in ratios similar to those of the polysaccharide from culture filtrates. Polysaccharide purified from noninfected cabbage leaves contained only glucose and galactose. The polysaccharide from infected cabbage leaves was serologically related to polysaccharide from culture filtrates. In immunodiffusion tests both the polysaccharide fractions from culture filtrates and that from infected leaves reacted to give two precipitin bands with an antiserum to the polysaccharide from culture filtrates. No precipitin bands formed with polysaccharide from noninfected leaves. Antibodies against the culture polysaccharide were completely removed from the antiserum by the polysaccharides isolated from infected cabbage leaves. A weakly virulent isolate of X. campestris did not produce extracellular polysaccharide in culture filtrates.


2011 ◽  
Vol 284-286 ◽  
pp. 1742-1745 ◽  
Author(s):  
Ming Ye ◽  
Xiao Chen ◽  
Guang Wei Li ◽  
Geng Yi Guo ◽  
Liu Yang

Melanin was isolated from the mycelium of Lachnum singerianum YM-292 (LSM) by alkaline extraction, acid hydrolysis, and repeated precipitation with a yield of 8.85 g/100 g (dry weight basis). Scanning electron microscopy showed that LSM had a blocky crystal structure with an irregular surface. The percentages of C, H, N, O and S in LSM measured by the elemental analyzer were 54.44%, 6.65%, 8.25%, 24.24% and 6.42%, respectively. Infrared spectroscopy indicated that LSM had a typical indole structure, and1H-NMR spectroscopy revealed signal peaks in the aliphatic and aromatic regions. It was concluded that LSM had a structural model of pheomelanin-like pigment.


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