Stability of a cylindrical plasma in the presence of a monotonic field-II

The stability of an incompressible inviscid, perfectly conducting cylindrical plasma against azimuthal disturbances in the presence of a monotonic decreasing magnetic field having a constant pitch is discussed by using energy principle. The results obtained by this principle are compared for m = 1 mode (which is a dangerous mode in which there is a lateral shift of the entire column) with that obtained by normal mode analysis. It is found that m = 1 mode is always unstable. Further, an axial line current, external axial field and the surface tension tend to stabilise m ≠ modes.

Stability of systems with power-law non-linearities

It is shown that a sufficient condition for the asymptotic stability-in-the-large of an autonomous system containing a linear part with transfer function G(jω) and a non-linearity belonging to a class of power-law non-linearities with slope restriction [0, K] in cascade in a negative feedback loop is ReZ(jω)[G(jω) + 1 K] ≥ 0 for all ω where the multiplier is given by, Z(jω) = 1 + αjω + Y(jω) - Y(-jω) with a real, y(t) = 0 for t < 0 and ∫ 0 ∞ |y(t)|dt < 1 2c2, c2 being a constant associated with the class of non-linearity. Any allowable multiplier can be converted to the above form and this form leads to lesser restrictions on the parameters in many cases. Criteria for the case of odd monotonic non-linearities and of linear gains are obtained as limiting cases of the criterion developed. A striking feature of the present result is that in the linear case it reduces to the necessary and sufficient conditions corresponding to the Nyquist criterion. An inequality of the type |R(T) - R(- T)| ≤ 2c2R(0) where R(T) is the input-output cross-correlation function of the non-linearity, is used in deriving the results.

Nature, stability and bonding of the peroxy group in peroxy titanium compounds

Some physicochemical properties of peroxy titanium compounds are explained by assigning a strained triangular ring structure to the peroxy titanyl group, with a bent and reduced overlap of the O---O bonding orbitals. The stability of the peroxy group is found to depend on the stability of the other ligands. The decreasing order of stability of the peroxy group in the compounds is as: oxalato > meleato > malonato > sulphato > peroxide of titanium.

Studies on the enzyme hydrolysing flavin mononucleotide in plants: I. Partial purification and properties of the enzyme from Phaseolus radiatus

The partial purification of the enzyme hydrolysing FMN from extracts of greengram seeds (Phaseolus radiatus) is described. The procedures, which entailed precipitation of inert material by manganous sulfate and protamine sulfate treatment, fractional precipitation with alcohol and chromatography on CM-cellulose, afforded preparations whose specific activity was 200 times that of the initial crude extract. The preparation was comparatively specific for FMN. It also hydrolysed, to a much smaller extent, β-glycerophosphate, p-nitrophenyl phosphate and 5′-nucleotides. The differential effects of ions on the FMN and β-glycerophosphate hydrolysing activities are discussed.

Studies on the enzyme hydrolysing flavin mononucleotide in plants. I. Partial purification and properties of the enzyme from Phaseolus radiatus

The partial purification of the enzyme hydrolysing FMN from extracts of greengram seeds (Phaseolus radiatus) is described. The procedures, which entailed precipitation of inert material by manganous sulfate and protamine sulfate treatment, fractional precipitation with alcohol and chromatography on CM-cellulose, afforded preparations whose specific activity was 200 times that of the initial crude extract. The preparation was comparatively specific for FMN. It also hydrolysed, to a much smaller extent, β-glycerophosphate, p-nitrophenyl phosphate and 5′-nucleotides. The differential effects of ions on the FMN and β-glycerophosphate hydrolysing activities are discussed.

Studies on the enzyme hydrolysing flavin mononucleotide in plants: II. Phosphotransferase activity of the partially purified enzyme from Phaseolus radiatus

The preparation of the enzyme hydrolysing FMN whose partial purification from green-gram extracts is described in the preceding paper, has been shown to possess phosphotransferase activity. The enzyme could transfer the phosphate group cleaved from FMN to acceptors like thiamine, pyridoxal, pyridoxamine and nucleosides resulting in the formation of their corresponding phosphate esters and nucleotides. The properties of the enzyme hydrolysing FMN and the phosphotransferase activity of the preparation are compared.

Indoleacetaldoxime hydro-lyase (4.2.1.29). III. Further studies on the nature and mode of action of the enzyme

Further purification of indoleacetaldoxime (IAOX) hydro-lyase from Gibberella fujikuroi by DEAE-cellulose chromatography is described. The purified enzyme was activated by dehydroascorbic acid (DHA), ascorbic acid (AA), and pyridoxal phosphate (PALP) and was inhibited by thiol compounds and thiol reagents including phenylthiocyanate. Ferrous ions but not ferric ions activated the purified enzyme. The enzyme was activated by dihydrofolic acid but inhibited by tetrahydrofolic acid. Phenylacetaldoxime, a competitive inhibitor, afforded partial protection of the enzyme from the action of N-ethylmaleimide suggesting the involvement of a thiol function at the active site or substrate-binding site. The inhibition of the enzyme by 2,3-dimercaptopropanol was reversed by DHA, PALP, or frozen storage. KCN inhibition of the enzyme was reversed by PALP. NaBH4 reduction of the purified enzyme in the presence of PALP gave an active enzyme which was further activated by PALP or DHA but not by ferrous ions. These results suggested a "structural" role for PALP in the activity of IAOX hydro-lyase. Dilute solutions of the purified enzyme, obtained during DEAE-cellulose chromatography and concentrated using sucrose, showed enhanced activity upon frozen storage and thawing. The increase in activity of the enzyme during certain culture conditions, the activation and inhibition of the enzyme by several unrelated compounds, and the effect of freezing indicate that IAOX hydro-lyase is probably a metabolically regulated enzyme with a structure composed of subunits.

Role of entropy in the stability of cobalt titanates

The standard molar Gibbs free energy of formation of Co2TiO4, CoTiO3,and CoTi2O5 as a function of temperature over an extended range (900 to 1675) K was measured using solid-state electrochemical cells incorporating yttria-stabilized zirconia as the electrolyte, with CoO as reference electrode and appropriate working electrodes. For the formation of the three compounds from their component oxides CoO with rock-salt and TiO2 with rutile structure, the Gibbs free energy changes are given by:Delta(f)G degrees((ox))(Co2TiO4) +/- 104/(J . mol(-1)) = -18865 - 4.108 (T/K)Delta(f)G degrees((ox))(CoTiO3) +/- 56/(J . mol(-1)) = -19627 + 2.542 (T/K) Delta(f)G degrees((ox))(CoTi2O5) +/- 52/(J . mol(-1)) = -6223 - 6.933 (T/K) Accurate values for enthalpy and entropy of formation were derived. The compounds Co2TiO4 with spinel structure and CoTi2O5 with pseudo-brookite structure were found to be entropy stabilized. The relatively high entropy of these compounds arises from the mixing of cations on specific crystallographic sites. The stoichiometry of CoTiO3 was confirmed by inert gas fusion analysis for oxygen. Because of partial oxidation of cobalt in air, the composition corresponding to the compound Co2TiO4 falls inside a two-phase field containing the spinet solid solution Co2TiO4-Co3O4 and CoTiO3. The spinel solid solution becomes progressively enriched in Co3O4 with decreasing temperature. (c) 2010 Elsevier Ltd. All rights reserved.

Studies on nucleotide pyrophosphatase I. Partial purification and properties of a sheep liver enzyme that catalyzes the hydrolysis of dinucleotides

A partially purified sheep liver enzyme that hydrolyzed dinucleotides at the pyrophosphate bond was obtained by solubilizing the 18,000g sediment with n-butanol and fractionating the solubilized enzyme with acetone. The enzyme activity when measured using FAD as substrate, (FAD → FMN + AMP), was optimal at pH 9.7 and temperatures between 30 °–36 ° and at 60 °. The rate of release of FMN with time occurred with an initial lag of 30 sec, a linear increase for 1 min, and a subsequent irregular rate. In the presence of orthophosphate (Pi; 10 μImage ), FMN was released at an uniformly continuous and enhanced rate. 32Pi was not incorporated into the substrate or products. Sodium arsenate counteracted the effects of Pi. The apparent Km and Vmax were 0.133 mImage and 100 units; and 0.133 mImage and 200 units, in the absence and presence of Pi, respectively. The temperature optimum was 42 ° in the presence of Pi.Negative cooperative interactions observed at low concentrations of FAD were abolished by the addition of Pi. The inhibition by AMP was sigmoid and Pi abolished this sigmoidal response. The enzyme hydrolyzed in addition to FAD, NAD+ and NADP+. Nucleoside triphosphates were potent inhibitors of the enzyme activity. The partial inhibition of the enzyme by o-phenanthroline and by p-hydroxymercuribenzoate could be reversed by Fe2+ ions and by reduced glutathione, respectively.

Improved Conditions For L2-Stability Of Nonstationary Feedback-Systems

Concerning the L2-stability of feedback systems containing a linear time-varying operator, some of the stringent restrictions imposed on the multiplier as well as the linear part of the system, in the criteria presented earlier, are relaxed.

L2-Stability Of A Class Of Nonlinear-Systems

Sufficient conditions are given for the L2-stability of a class of feedback systems consisting of a linear operator G and a nonlinear gain function, either odd monotone or restricted by a power-law, in cascade, in a negative feedback loop. The criterion takes the form of a frequency-domain inequality, Re[1 + Z(jω)] G(jω) δ > 0 ω ε (−∞, +∞), where Z(jω) is given by, Z(jω) = β[Y1(jω) + Y2(jω)] + (1 − β)[Y3(jω) − Y3(−jω)], with 0 β 1 and the functions y1(·), y2(·) and y3(·) satisfying the time-domain inequalities, ∝−∞+∞¦y1(t) + y2(t)¦ dt 1 − ε, y1(·) = 0, t < 0, y2(·) = 0, t > 0 and ε > 0, and , c2 being a constant depending on the order of the power-law restricting the nonlinear function. The criterion is derived using Zames' passive operator theory and is shown to be more general than the existing criteria

Mandelic Acid 4-Hydroxylase - New Inducible Enzyme From Pseudomonas-Convexa

A soluble fraction of catalyzed the hydroxylation of mandelic acid to -hydroxymandelic acid. The enzyme had a pH optimum of 5.4 and showed an absolute requirement for Fe2+, tetrahydropteridine, NADPH. -Hydroxymandelate, the product of the enzyme reaction was identified by paper chromatography, thin layer chromatography, UV and IR-spectra

Oxidation of catechol in plants : III. Purification and properties of the diphenylene dioxide 2,3-quinone-forming enzyme system from Tecoma leaves

In attempting to determine the nature of the enzyme system mediating the conversion of catechol to diphenylenedioxide 2,3-quinone, in Tecoma leaves, further purification of the enzyme was undertaken. The crude enzyme from Tecoma leaves was processed further by protamine sulfate precipitation, positive adsorption on tricalcium phosphate gel, and elution and chromatography on DEAE-Sephadex. This procedure yielded a 120-fold purified enzyme which stoichiometrically converted catechol to diphenylenedioxide 2,3-quinone. The purity of the enzyme system was assessed by polyacrylamide gel electrophoresis. The approximate molecular weight of the enzyme was assessed as 200,000 by gel filtration on Sephadex G-150. The enzyme functioned optimally at pH 7.1 and at 35 °C. The Km for catechol was determined as 4 × 10−4 Image . The enzyme did not oxidize o-dihydric phenols other than catechol and it did not exhibit any activity toward monohydric and trihydric phenols and flavonoids. Copper-chelating agents did not inhibit the enzyme activity. Copper could not be detected in the purified enzyme preparations. The purified enzyme was not affected by extensive dialysis against copper-complexing agents. It did not show any peroxidase activity and it was not inhibited by catalase. Hydrogen peroxide formation could not be detected during the catalytic reaction. The enzymatic conversion of catechol to diphenylenedioxide 2,3-quinone by the purified Tecoma leaf enzyme was suppressed by such reducing agents as GSH and cysteamine. The purified enzyme was not sensitive to carbon monoxide. It was not inhibited by thiol inhibitors. The Tecoma leaf was found to be localized in the soluble fraction of the cell. Treatment of the purified enzyme with acid, alkali, and urea led to the progressive denaturation of the enzyme.