Über eine neue Gruppe von krystallin‐flüssigen Substanzen, die homologen p, p′‐Diphenyl‐pyridazine

Weygand, C.; Lanzendorf, W.

doi:10.1002/prac.19381510609

Cited by 33 publications

(16 citation statements)

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“…The reference 4,4 †-dipentyl-p-terphenyl (11) (51), the substituted 4,4 †-dipentyl-p-terphenyls (12)(13)(14)(15) (52,53) and the nitrogen heterocycles (16-18) (54-56) collated in Table 4 are rigid and consist of three six-membered aromatic rings in a linear configuration with two pentyl chains in para-positions situated on the terminal phenyl rings (22,(49)(50)(51)(52)(53)(54)(55)(56)(57)(58). This molecular structure is characterised by a high degree of symmetry and a limited degree of shape anisotropy.…”

Section: Transition Temperaturesmentioning

confidence: 99%

Rod-shaped dopants for flexoelectric nematic mixtures

et al. 2009

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We report the synthesis and liquid crystalline behaviour of two series of para-substituted terphenyls as dopants with a rigid rod-like shape, rather than a wedge-, pear-or banana-shape, for guest-host nematic mixtures with flexoelectric properties. One series of liquid crystalline dopants is of low-to-strongly negative dielectric anisotropy and the other is of low-to-strongly positive dielectric anisotropy. The usefulness of apolar and polar rod-like dopants as components of flexoelectric nematic mixtures of positive dielectric anisotropy for use in LCDs is investigated in general and the dependence of the flexoelectric properties of the doped nematic mixtures on the polarity of the dopants is studied in particular. The correlation between the concentration of the dopant and the magnitude of the flexoelastic ratio of several guest-host nematic mixtures is investigated.

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Section: Transition Temperaturesmentioning

confidence: 99%

Rod-shaped dopants for flexoelectric nematic mixtures

et al. 2009

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“…The peptides obtained were purified by chromatography on a silica gel column in the system butan-1-al/acetic acid/pyridine/water (15:3: 10: 12, v/v/v/v). Trifluoroacetyl derivatives were obtained as in [9].…”

Section: Methodsmentioning

confidence: 99%

Study of the specificity of histone kinase using synthetic substrates

et al. 1978

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“…6-Diazo-5-oxo-~-norleucine was synthesized as reported previously [13] by the method described by Weygand and Reiher [20,21].…”

Section: Synthesis Of 6-diazo-5-oxo-~-norleucinementioning

confidence: 99%

Latent Active Site in Rat-Kidney gamma-Glutamyl Transpeptidase. The Refolding Process of the Large Subunit and Characterization of the Renatured Enzyme

1980

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Rat kidney y-glutamyl transpeptidase (EC 2.3.2.2) is composed of two non-identical subunits (the large and small subunits). In the native state of this enzyme, the active site resides on the small subunit. The present investigation has been performed to confirm and extend in further detail the previously described finding that the large subunit isolated from the native dimeric enzyme is also catalytically active [S. Horiuchi, M. Inoue and Y. Morino (1978) Biochem. Biophys. Res. Commun. 80,873 -8781. A pure preparation of y-glutamyl transpeptidase which had been completely inactivated by affinity labeling with 6-diazo-5-oxo-~-norleucine was dissociated into the small subunit and the large subunit under denaturating conditions. Upon renaturation, only the large subunit restored the enzymic activity.Sephadex G-200 column chromatography of the renatured preparation of the large subunit revealed the presence both of enzymically inactive aggregate forms and the enzymically active species. The enzymically active molecules of the renatured large subunit behaved as particles having a molecular weight of 48000 2 2000. This indicates that the enzymically active species of the large subunit has a monomeric structure.Under the present experimental conditions, the restoration of enzymic activity of the large subunit was optimal at a protein concentration of approximately 150 pg/ml and seemed to require the presence of glutathione or its S-methyl derivative as a substrate ligand.The restoration of the enzymic activity of the large subunit was accompanied by a conformational change as judged by both circular dichroic and immunochemical properties.Some kinetic properties of the reaction with y-glutamyl-p-nitroanilide and the affinity label, 6-diazo-5-oxo-~-norleucine were essentially identical between the renatured large subunit and the native oligomeric enzyme. y-Glutamyl transpeptidase catalyzes the transfer reaction of a y-glutamyl moiety of glutathione or S-substituted glutathione derivatives to acceptors such as amino acids and peptides [1,2]. Many proposals have been made on the possible participation of this enzyme in physiological functions, including ammoniagenesis in metabolic acidosis [3,4], mercapturate biosynthesis [5,6], amino acid and peptide transport [7 -91 and so forth. Rat kidney y-glutamyl transpeptidase consists of two non-identical subunits (the large and small subunit) [lo-121. The small subunit has been shown to have an active site which is labeled by 6-diazo-5-oxo-~-norleucine, an affinity label for this enzyme [13,14], suggesting that the small subunit is a catalytic component of the enzyme. However, little has been known about the functional Enzyme. y-Glutamyl transpeptidase (EC 2.3.2.2) aspect of the large subunit except that this subunit may be mainly involved in anchoring this membranous enzyme into the renal brush border membrane [ l l , 12,151.When we studied subunit-subunit interaction of y-glutamyl transpeptidase to gain an insight into the possible functional role of the large subunit, a re...

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Über eine neue Gruppe von krystallin‐flüssigen Substanzen, die homologen p, p′‐Diphenyl‐pyridazine

Cited by 33 publications

References 0 publications

Rod-shaped dopants for flexoelectric nematic mixtures

Rod-shaped dopants for flexoelectric nematic mixtures

Study of the specificity of histone kinase using synthetic substrates

Latent Active Site in Rat-Kidney gamma-Glutamyl Transpeptidase. The Refolding Process of the Large Subunit and Characterization of the Renatured Enzyme

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