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Studies of rabbit brain, intestine and liver guanine aminohydrolase
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1984Guanine aminohydrolase (EC 3.5.4.3) from rabbit brain, intestine, and liver has been purified to homogeneity by affinity chromatography at room temperature and 0-4 degrees C. In all cases the recovery and fold purification was greatest for purification at room temperature. Each enzyme has a subunit mol.
M E, Pugh, A L, Bieber
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Adenosine aminohydrolase activity in the regenerating rat liver
Archives of Biochemistry and Biophysics, 1985The 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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Cytidine aminohydrolase activity in intact cultured transformed cells
Journal of Cellular Physiology, 1968AbstractCultures of several cell lines convert cytidine, if present in their medium, to uridine. The reaction is rapid, being virtually complete within one hour. The enzymatic activity is that of cytidine aminohydrolase (EC 3.5.4.5). The activity is exhibited by the intact cell — substrate and products being found in the medium bathing the cells.
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Pattern of product inhibition of 5′-AMP aminohydrolase
Archives of Biochemistry and Biophysics, 1974Abstract 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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[Various properties of immobilized AMP-aminohydrolase].
Ukrainskii biokhimicheskii zhurnal (1978), 1986Properties of immobilized AMP-aminohydrolase from rabbit muscles are studied. The enzyme retains its activity for a year, is stable under manifold treatment with the substrate or under single treatment with 1 M NaCl which contains 50% ethylene glycol or 10% isopropanol and under treatment with 5 M K2 HPO4 (pH 8.5).
V A, Tugaĭ, A P, Ignatchenko
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Biochimica et Biophysica Acta (BBA) - Protein Structure, 1972
A. Raggi +3 more
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A. Raggi +3 more
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[Molecular forms of guanine aminohydrolase (author's transl)].
Revista espanola de fisiologia, 1978Guanine aminohydrolase (E.C. 3.5.4.3) has been purified 11-fold from the supernatant fraction of guinea-pig liver homogenates in 0.25 M sucrose (centrifuged at 50,000 X g) through thermic denaturation at 60 degrees C and ammonium sulphate fractionation (30--60% saturation). The enzyme in the homogenates and purified preparations exhibited two Km values.
L, Martínez-Farnós +2 more
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Circannual variation in human erythrocyte adenosine aminohydrolase.
Chronobiologia, 1978In serially independent samples of blood from apparently healthy subjects controlled as to clock-hour of blood withdrawal but not as to any circannual changes in circadian state, human erythrocyte adenosine aminohydrolase undergoes a statistically significant circannual rhythm, which may or may not be aliased.
A, Nechaev +3 more
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Conformational isomers of deoxycytidylate aminohydrolase
Biochemistry, 1971Eduardo Scarano +4 more
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Adenosine aminohydrolase from Streptomyces aureofaciens
Collection of Czechoslovak Chemical Communications, 1978Magdaléna Rosinová +2 more
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