Calculation of electro-optical parameters, a new approach. Part III. Applications to X<SUB>2</SUB>CZ molecules (X=H, F, Cl, Br and Z=O, S)

Calculations of electro-optical parameters by the modified first order approximation (MFOA) method have been extended to X2CZ (X=H, F, Cl, Br; Z=O, S) molecules with a view to investigate the transferability of these parameters. The diagonal and cross elements of the bond moment derivative matrix have been evaluated. Unique values of &#956;C-X are obtained for the A1 species. The bond moment derivatives are found to be transferable among A1 and B1 species. Transferability of the &#956;C-Z in B1 and B2 species is obtained for thiocarbonyl halides. Bond moment derivatives with respect to angle deformations are not found to be very significant whereas other cross elements of the bond moment derivative matrix are found to be of high magnitude

Compounds of Uranyl Chloride with Monoamines

Compounds of uranyl chloride with monoamines were prepared in non-aqueous solvents. Their properties have been studied and structure discussed

Study of self-similar and steady flows near singularities. II. A case of multiple characteristic velocity

We consider here a system of first-order quasilinear partial differential equations in two independent variables: t, time and x, spatial coordinate. In many physically realistic problems in fluid mechanics, a singularity of the system of ordinary differential equations representing the steady solutions represents a critical state where one of the characteristic velocities vanishes (e.g. sonic point in fluid mechanics). Kulikovskii &amp; Slobodkina (1967) have shown that the stability of all the steady solutions near a singularity can be studied with the help of a simple first-order quasi-linear partial differential equation. The simplicity of their method lies in the fact that all the results can be deduced from the phase-plane of the steady equations. The analysis of Kulikovskii &amp; Slobodkina is valid for any system of equations, totally hyperbolic or mixed type with the only assumption that the characteristic velocity under consideration is real and not multiple. We have earlier (1970, to be referred to as part I) extended their treatment to self-similar flows. In this paper we have shown that in the case of a characteristic velocity of multiplicity s (s &gt; 1), it is still possible to approximate the system provided there exists exactly s linearly independent eigenvectors corresponding to this characteristic velocity. The approximate system consists of s quasi-linear equations and we have to consider the s + 1 dimensional phase-space of the steady equations. In the end we have also discussed two illustrative examples

Study of self-similar and steady flows near singularities

One-dimensional steady state flow or a self-similar flow is represented by an integral curve of the system of ordinary differential equations and, in many important cases, the integral curve passes through a singular point. Kulikovskii &amp; Slobodkina (1967) have shown that the stability of a steady flow near the singularity can be studied with the help of a simple first-order partial differential equation. In section 2 of this paper we have used their method to study steady transonic flows in radiation-gas-dynamics in the neighbourhood of the sonic point. We find that all possible one-dimensional steady flows in radiation-gas-dynamics are locally stable in the neighbourhood of the sonic point. A continuous disturbance on a steady flow, while decaying and propagating, may develop a surface of discontinuity within it. We have determined the conditions for the appearance of such a discontinuity and also the exact position where it appears. In section 3 we have shown that their method can be easily generalized to study the stability of self-similar flows. As an example we have considered the stability of the self-similar flow behind a strong imploding shock. In this case we find that the flow is stable with respect to radially symmetric disturbances

Purification and characterization of arginine decarboxylase from cucumber (Cucumis sativus) seedlings

A simple, reproducible and rapid protocol for the purification of arginine decarboxylase fromCucumis sativus seedlings has been standardised. The purification steps involved ion-exchange chromatography on diethylaminoethyl-cellulose followed by gel filtration on Sephadex G-l 50. The purified enzyme preparation migrated as a single stainable band on Polyacrylamide gels at both basic and acidic pH, but under denaturing and reducing conditions on sodium dodecyl sulphate-polyacrylamide gels resolved into polypeptides of molecular weight 48,000,44,000 and 15,000. However, in the absence of 2-mercaptoethanol on electrophoresis on sodium dodecyl sulphate-polyacrylamide gels, the enzyme moved as single band with a molecular weight of 150,000. Evidence was obtained to indicate that these three polypeptides were probably derived from a single larger molecular weight enzyme. On storage of the purified protein, the 48,000 species was preferentially degraded to smaller polypeptides. The preliminary data suggested that the 48,000 and 44,000 species shared many common tryptic peptides as revealed by finger printing of the [125I ]-labelled protein. The purified enzyme was a glycoprotein and had a Km of 0.5 mM for arginine. Its activity was stimulated by dithiothrietol and pyridoxal phosphate. EDTA did not inhibit the enzyme activity. Mn2+ at 1 mM stimulated arginine decarboxylase activity but was inhibitory at higher concentration

Decarboxylation of arginine and ornithine by arginine decarboxylase purified from cucumber (Cucumis sativus) seedlings

A purified preparation of arginine decarboxylase fromCucumis sativus seedlings displayed ornithine decarboxylase activity as well. The two decarboxylase activities associated with the single protein responded differentially to agmatine, putrescine andPi. While agmatine was inhibitory (50 %) to arginine decarboxylase activity, ornithine decarboxylase activity was stimulated by about 3-fold by the guanido arnine. Agmatine-stimulation of ornithine decarboxylase activity was only observed at higher concentrations of the amine. Inorganic phosphate enhanced arginine decarboxylase activity (2-fold) but ornithine decarboxylase activity was largely uninfluenced. Although both arginine and ornithine decarboxylase activities were inhibited by putrescine, ornithine decarboxylase activity was profoundly curtailed even at 1 mM concentration of the diamine. The enzyme-activated irreversible inhibitor for mammalian ornithine decarboxylase,viz. α -difluoromethyl ornithine, dramatically enhanced arginine decarboxylase activity (3-4 fold), whereas ornithine decarboxylase activity was partially (50%) inhibited by this inhibitor. At substrate level concentrations, the decarboxylation of arginine was not influenced by ornithine andvice-versa. Preliminary evidence for the existence of a specific inhibitor of ornithine decarboxylase activity in the crude extracts of the plant is presented. The above results suggest that these two amino acids could be decarboxylated at two different catalytic sites on a single protein

Purification and characterization of putrescine synthase from cucumber seedlings. A multifunctional enzyme involved in putrescine biosynthesis

The multifunctional enzyme, putrescine synthase has been purified fromCucumis sativus and characterized. This enzyme harbours agmatine iminohydrolase, ornithine transcarbamylase, putrescine transcarbamylase and carbamate kinase activities, whose concerted action results in agmatine → putrescine conversion. The enzyme resolved into two aggregation forms, enzyme aggregated and enzyme monomer upon electrophoresis at pH 8.3. Evidence has been provided by two-dimensional gel electrophoresis that both enzyme aggregated and enzyme monomer comprise of identical polypeptide chains. Under non-reducing conditions on sodium dodecyl sulphate-polyacrylamide gel electrophoresis, the protein moves as a single 150 KDa polypeptide; however, in the presence of 2-mercaptoethanol on sodium dodecyl sulphate-polyacrylamide gel elec trophoresis, it migrates as 3 polypeptides of molecular weight 48,000, 44,000 and 15,000. The enzyme undergoes age-dependentin vivo proteolytic degradation from a 66 KDa polypeptide (primary translational product), through 48 KDa polypeptide to 44 KDa species and finally to small molecular weight peptides