Boxicity and separation dimension

A family $\mathcal{F}$ of permutations of the vertices of a hypergraph $H$ is called 'pairwise suitable' for $H$ if, for every pair of disjoint edges in $H$, there exists a permutation in $\mathcal{F}$ in which all the vertices in one edge precede those in the other. The cardinality of a smallest such family of permutations for $H$ is called the 'separation dimension' of $H$ and is denoted by $\pi(H)$. Equivalently, $\pi(H)$ is the smallest natural number $k$ so that the vertices of $H$ can be embedded in $\mathbb{R}^k$ such that any two disjoint edges of $H$ can be separated by a hyperplane normal to one of the axes. We show that the separation dimension of a hypergraph $H$ is equal to the 'boxicity' of the line graph of $H$. This connection helps us in borrowing results and techniques from the extensive literature on boxicity to study the concept of separation dimension.Comment: This is the full version of a paper by the same name submitted to WG-2014. Some results proved in this paper are also present in arXiv:1212.6756. arXiv admin note: substantial text overlap with arXiv:1212.675

Arginine decarboxylase is a component activity of the multifunctional enzyme putrescine synthase in cucumber seedlings

A homogenous PreParation of Putrescine synthase, the versatile multifunctional enzyme involved in agmatine →Putrescine conversion inCucumis sativus was found to catalyze enzymatic decarboxylation of arginine also. Similarly, the Purified arginine decarboxylase mediated the comPonent as well as the comPlete set of couPled reactions harboured by Putrescine synthase. Both the enzyme PreParations exhibited identical electroPhoretic and chromatograPhic behaviour and were immunologically indistinguishable. All the enzymic activities are stabilized concurrently by feeding arginine to the intact seedlings. Therefore, it is concluded that the multifunctional Putrescine synthase inCucumis sativus seedlings also harbours arginine decarboxylase activity unlike its counterPart in Lathyrus sativus

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

Biosynthesis and regulation of polyamines in higher plants

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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

Vibrational Stability of NLC Linac accelerating structure

The vibration of components of the NLC linac, such as accelerating structures and girders, is being studied both experimentally and analytically. Various effects are being considered including structural resonances and vibration caused by cooling water in the accelerating structure. This paper reports the status of ongoing work.Comment: 3 pages 8 figures Presented at EPAC 2002 Paris Franc

Griffiths phase-like behaviour and spin-phonon coupling in double perovskite Tb2_{2}NiMnO6_{6}

The Griffiths phase-like features and the spin-phonon coupling effects observed in Tb$_2$NiMnO$_6$ are reported. The double perovskite compound crystallizes in monoclinic $P2_1/n$ space group and exhibits a magnetic phase transition at $T_c \sim$ 111 K as an abrupt change in magnetization. A negative deviation from ideal Curie-Weiss law exhibited by 1/$\chi(T)$ curves and less-than-unity susceptibility exponents from the power-law analysis of inverse susceptibility are reminiscent of Griffiths phase-like features. Arrott plots derived from magnetization isotherms support the inhomogeneous nature of magnetism in this material. The observed effects originate from antiferromagnetic interactions which arise from inherent disorder in the system. Raman scattering experiments display no magnetic-order-induced phonon renormalization below $T_c$ in Tb$_2$NiMnO$_6$ which is different from the results observed in other double perovskites and is correlated to the smaller size of the rare earth. The temperature evolution of full-width-at-half-maximum for the {\it stretching} mode at 645 cm$^{-1}$ presents an anomaly which coincides with the magnetic transition temperature and signals a close connection between magnetism and lattice in this material.Comment: 17 pages, 8 figures; accepted in J. Appl. Phy

Vibrational Stability of NLC Linac and Final Focus Components

Vertical vibration of linac components (accelerating structures, girders and quadrupoles) in the NLC has been studied experimentally and analytically. Effects such as structural resonances and vibration caused by cooling water both in accelerating structures and quadrupoles have been considered. Experimental data has been compared with analytical predictions and simulations using ANSYS. A design, incorporating the proper decoupling of structure vibrations from the linac quadrupoles, is being pursued.Comment: 3 pages, 8 figures presented at the LINAC 2002 conference, Gyeongju Kore

Effect of Cooling Water on Stability of NLC Linac Components

Vertical vibration of linac components (accelerating structures, girders and quadrupoles) in the NLC has been studied experimentally and analytically. Effects such as structural resonances and vibration caused by cooling water both in accelerating structures and quadrupoles have been considered. Experimental data has been compared with analytical predictions and simulations using ANSYS. A design, incorporating the proper decoupling of structure vibrations from the linac quadrupoles, is being pursued.Comment: 6 Pages 13 Figures Presented at The Nanobeam 2002 Workshop (Lausanne Switzerland