Results 191 to 200 of about 1,080,434 (247)

Chemistry and Mechanism of Urease Inhibition

Current Medicinal Chemistry, 2002
Studies on enzyme inhibition remain an important area of pharmaceutical research since these studies have led to the discoveries of drugs useful in a variety of physiological conditions. The enzyme inhibitors can interact with enzymes and block their activity towards natural substrates.
Z, Amtul, Atta-Ur, Rahman, R A, Siddiqui, M I, Choudhary   +3 more
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Quantitative studies on the inhibition of crystalline urease by rabbit anti-urease

Archives of Biochemistry and Biophysics, 1955
Abstract 1. 1. Quantitative precipitin studies with crystalline urease and antiurease have been performed. The resulting data provide information concerning the combining proportions of the enzyme and antibody on a weight basis. 2. 2. Urease is inhibited by rabbit anti-urease. 3. 3.
A A, MARUCCI, M M, MAYER
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The inhibition of urease and proteases by sodium saccharin

Cancer Letters, 1982
Sodium saccharin, at concentrations similar to those in the urine of rats fed 1-5% sodium saccharin in their diet, markedly inhibited urease, and 3 proteases in vitro and sodium ion did not appear to play a role in enzyme inhibition. These observations suggest that enzyme inhibition of any of a large number of enzymes may play a role in the ...
E, Lok, F, Iverson, D B, Clayson
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Inhibition of urease by hydroxyurea

Biochemical Pharmacology, 1965
Abstract Hydroxyurea was shown to be a potent inhibitor of urease; 50% inhibition occurred at a concentration of approximately 5 × 10−5 M. Preincubation of the enzyme with the inhibitor prior to addition of substrate yielded inhibition which progressed with time, whereas simultaneous addition of inhibitor and substrate to the enzyme reduced the ...
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Inhibition of soybean urease by polycarbonyl compounds

Applied Biochemistry and Microbiology, 2005
Competitive inhibition of soybean urease was studied at 36 degrees C in aqueous solution (pH 4.95) in the presence of polycarbonyl compounds (PCCs): oxalyldihydrazide (ODH), its polydisulfide (poly(DSODH)), three cyclic beta-triketones (CTKs), and seven cyclic PCC species of differing structure.
E I, Tarun, D B, Rubinov, D I, Metelitsa
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Inhibition of Urease by Alloxan and Alloxanic Acid

Nature, 1959
EVER since the discovery that alloxan could induce diabetes1 in animals, this compound has been the agent of choice in producing experimental diabetes. While the maximal modifications in the chemical structure of alloxan compatible with maintenance of diabetogenic action are known, its mode of action is still debated.
C T, GRAY, M S, BROOKE, J C, GERHART
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Inhibition of soybean urease by triketone oximes

Biochemistry (Moscow), 2004
Competitive inhibition of soybean urease by 15 triketone oximes has been studied at 36 degrees C in aqueous solution (pH 4.95). The studied oximes are supposed chelators for the nickel atom in the urease metallocenter. The inhibition constants of urea hydrolysis (K(i)) varied in the range 2.7-248 microM depending on the oxime structure.
E I, Tarun, D B, Rubinov, D I, Metelitza
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Urease inhibition by hydroxamic acids

Experientia, 1981
Ureases from jack beans andRhodototorula pilimanae were observed to be inhibited by primary hydroxamic acids but were not inhibited by acyclic-secondary (N-alkyl) hydroxamic acids.
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Specific Inhibition of Urease by N-Acylphosphoric Triamides

The Journal of Biochemistry, 1985
Benzoyl- and isopentenoyl phosphoric triamides (BPA and IPA) strongly inhibited urease activities from jack bean, soybean, watermelon seed, Proteus mirabilis, P. rettgeri, P. vulgaris, Mycobacterium smegmatis, and Ureaplasma urealyticum. Their I50 values (the final concentration causing 50% inhibition), independent of enzyme source, were 2-21 nM, which
K, Kobashi, S, Takebe, A, Numata
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