Results 101 to 110 of about 756 (126)

Isolation and Characterization of Leishmanial Adenine Aminohydrolase as a Drug Target

Current Computer-Aided Drug Design, 2021
Background: Search for new drug targets is becoming imperative these days given that marketed chemotherapeutic drugs have lost their efficacy against harmful agents because of adaptability to climatic changes and co-evolving vectors to new hosts.
Firdous, Butt, Masoom, Yasinzai, Shaukat Iqbal, Malik, Anum, Munir   +3 more
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Nucleoside aminohydrolase, an enzyme involved in the degradation of deoxycytidine

Experientia, 1969
Hohe Nukleosidaminohydrolase-Aktivitaten finden sich in Niere, Leber und Darm von Hamstern. Bei Mausen hangt die Aktivitat vom Tierstamm ab und steht in Beziehung zur Deoxycytidinausscheidung.
B, Zicha, G B, Gerber, J, Deroo
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pH stat assay for guanine aminohydrolase

Analytical Biochemistry, 1971
Abstract A direct and continuous assay for guanine aminohydrolase has been developed that is based on the liberation of one mole of base for each mole of product formed. Direct continuous titration of the reaction at fixed pH with a standard solution of acid with a pH stat allows one to relate titration rate to rate of product formation.
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Freezing of dCMP aminohydrolase in the activated conformation by glutaraldehyde

Journal of Molecular Biology, 1978
Abstract dCMP aminohydrolase, which is an allosteric enzyme, was reacted with glutaraldehyde in the presence of the allosteric activator deoxycytidine-5′-triphosphate and of the competitive inhibitor deoxyadenosine-5′-monophosphate. The isolated modified enzyme is no longer sensitive to the effect of the allosteric ligands and shows kinetics typical ...
R, Nucci, C A, Rala, C, Vaccaro, S, Sepe, E, Scarano, M, Rossi   +5 more
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Esterase activity of 5′-adenosine monophosphate aminohydrolase

Archives of Biochemistry and Biophysics, 1975
Abstract 5′-AMP aminohydrolase (EC 3.5.4.6) was found to hydrolyze p -nitrophenyl acetate. The enzyme shows a normal saturation curve with this substrate. The transient kinetics revealed two fast processes followed by the slower steady-state rate of phenoxide release.
A C, Quenelle, W R, Melander
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The Purification of Rabbit Liver Guanine Aminohydrolase by Affinity Chromatography

Preparative Biochemistry, 1978
Abstract Rabbit liver guanine aminohydrolase (GAH) was purified 7100 fold to a specific activity of 35.5 units/mg with 60% yield. The three step purification involved homogenization at pH 5.0, 40–80% (NH4)∗S04 fractionation at pH 6.5 and affinity chromatography on 9-(p-aminoethoxyphenyl)guanine-Sepahros.e 48 (AEPGS).
J D, Bergstrom, A L, Bieber
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Adenosine aminohydrolase activity in the regenerating rat liver

Archives of Biochemistry and Biophysics, 1985
The specific activity of adenosine aminohydrolase in the regenerating rat liver is significantly increased 12 h after partial hepatectomy. There is a twofold increase in enzyme activity at 48 h, after which the activity begins to decline. However, increased values still persist 7 days postsurgery. The enzyme is located mainly in the soluble supernatant
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Adenosine aminohydrolase inhibition in cosolvent—Buffer mixtures

Archives of Biochemistry and Biophysics, 1974
Abstract Adenosine aminohydrolase from calf intestinal mucosa is sensitive to changes in the cooperative water structure of its environment as induced by the cosolvent dioxane. When dioxane is added to lower the dielectric constant from that of 78 of neat water to about 74, V is approximately halved, competitive inhibition by N6-(Δ2-isopentenyl ...
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POTENTIATION OF AMP‐AMINOHYDROLASE ACTIVITY OF BRAIN MITOCHONDRIA BY HEXOKINASE

Journal of Neurochemistry, 1971
Abstract— The addition of hexokinase (yeast and brain) to mitochondrial fractions of brain (rat) resulted in a considerable increase of formation of ammonia from AMP. The mechanisms underlying the activation of AMP‐aminohydrolase of brain mitochondria by ATP and hexokinase are quite different.
H C, Buniatian, A V, Haroutunian
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Pattern of product inhibition of 5′-AMP aminohydrolase

Archives of Biochemistry and Biophysics, 1974
Abstract The inhibition of 5′-AMP aminohydrolase (EC 3.5.4.6) by NH 4 Cl and IMP was examined. IMP was found to be a simple competitive inhibitor with respect to the substrate, AMP, while NH 4 Cl exhibited a pattern of inhibition with both noncompetitive and competitive elements. A number of possible mechanisms were analyzed.
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