Results 281 to 290 of about 40,476 (314)
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METABOLISM OF BENZIMIDAZOLE IN WHEAT: I. FORMATION OF BENZIMIDAZOLE NUCLEOTIDE

Canadian Journal of Biochemistry, 1965
An enzyme, probably benzimidazole nucleotide:pyrophosphate phosphoribosyl transferase, has been demonstrated in the 33–65% (NH4)2SO4fraction of wheat embryos. The enzyme was assayed indirectly by the apparent inhibition of the analogous orotidine-5′-phosphate pyrophosphorylase caused by benzimidazole competing with orotate for P-ribosyl-PP.
M. Kapoor, E. R. Waygood
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Prototropism in 2-acetyl benzimidazole and 2-benzoyl benzimidazole

Journal of Photochemistry and Photobiology A: Chemistry, 2005
2-Acetyl benzimidazole (2ABI) and 2-benzoyl benzimidazole (2BBI) are found to show excited state prototropic activities in different solvents of varying pH. The absorption, steady state and time-resolved emission studies were made on the basis of a theoretical possibility study of proton transfer in the excited state.
Sankar Chakravorti   +4 more
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Benzimidazoles: Veterinary uses

Parasitology Today, 1990
Benzimidazoles are valued for use against helminth infections in domestic animals. Here, Bill Campbell discusses efficacy, dosages, methods of administration and the species of parasite against which they are applied.
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Biochemistry of benzimidazole resistance

Acta Tropica, 1994
Heavy reliance on the benzimidazole (BZ) anthelmintics since their introduction in the 1960's for the control of gastrointestinal parasites of livestock has led to widespread BZ resistance in target parasite species. The BZs exert their primary action by binding to tubulin, the major protein component of microtubules.
Jennifer H. Gill, Ernest Lacey
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Oxomolybdenum (V) Complexes of Benzimidazole and 2 - Substituted Benzimidazoles

Synthesis and Reactivity in Inorganic and Metal-Organic Chemistry, 1991
Abstract Oxomolybdenum (V) complexes of the type (LH)2-[MoOCl5], (LH)2 [MoOCl4.OH], (LH)MOOCI4.F2O], [Mo2O4cl-(L - H)L′ (H2O)2-].nH2O, (where L = benzimidazole, 2 - α-hydroxymethyl benzimidazole, 2 - α - hydroxyethyl benzimidazole and 2 - α- hydroxybenzyl benzimidazole, L″ = EtOH or H2O and n = O, 1 or 2); [MoOCl3(L)2]H2O, (L = benzimidazole); [MoOCl2 ...
S. R. Girish, Vinayak B. Mahale
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Benzimidazole Ligands

ChemInform, 2003
AbstractFor Abstract see ChemInform Abstract in Full Text.
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Interaction of anthelmintic benzimidazoles and benzimidazole derivatives with bovine brain tubulin

Biochimica et Biophysica Acta (BBA) - General Subjects, 1978
The binding and inhibitory properties of 11 benzimidazoles for bovine brain tubulin were investigated. The effects of the benzimidazoles on the initial rates of microtubule polymerization were determined by a turbidimetric assay. The median inhibitory concentrations (I50) for nocodazole, oxibendazole, parbendazole, mebendazole and fenbendazole ranged ...
Paul A. Friedman, Edward G. Platzer
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Mode of action of benzimidazoles

Parasitology Today, 1990
Benzimidazoles represent the only class of truly broad-spectrum anthelmintics, however, they also show activity against fungi and mammalian cells. This raises the question as to why benzimidazoles can selectively kill helminths and yet exhibit little or no mammalian toxicity.
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ChemInform Abstract: 2H‐Benzimidazoles (Isobenzimidazoles). Part 3. Thermal Isomerization of Substituted 2H‐Benzimidazoles to 1H‐Benzimidazoles.

ChemInform, 1988
2H-Benzimidazole-2-spirocyclohexanes (1) when heated undergo a 1,5-sigmatropic rearrangement to 2,3-disubstituted 1H-benzimidazoles. A decided effect on the direction of this Isomerisation was observed with substituents in the homodiene ring.
Hans Suschitzky   +3 more
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Iron–sulphur dimers with benzimidazolate–thiolate, benzimidazolate–phenolate, or bis(benzimidazolate) terminal chelating ligands

J. Chem. Soc., Chem. Commun., 1986
[Fe2S2L2]2– complexes co-ordinated by the mixed-donor N–S, N–O, or N–N ligands L1–L4 are characterised by electronic and n.m.r. spectroscopy and shown to undergo one-electron reduction to the corresponding trianions with e.s.r. spectra exhibiting a range of g-tensor values which are compared with those for [2Fe–2S]+ proteins of the Rieske type.
Peter Beardwood, John F. Gibson
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