Results 131 to 140 of about 860 (163)

Adenosine-5'-monophosphate aminohydrolase of human placenta.

Acta biochimica Polonica, 1971
W, Makarewicz, E, Maćkowiak
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Characterization of purified guanine aminohydrolase

Archives of Biochemistry and Biophysics, 1979
Abstract Guanine aminohydrolase (GAH) (E.C. 3.5.4.3) was purified by affinity chromatography on 9-( p -β-aminoethoxyphenyl)guanine-Sepharose to a specific activity of 35.5 units/mg. The molecular weight of the enzyme was estimated to be 110,000 by gel filtration.
J D, Bergstrom, A L, Bieber
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Adenosine Aminohydrolase from Halobacterium cutirubrum

Canadian Journal of Biochemistry, 1973
The extreme halophilic bacterium Halobacterium cutirubrum was examined for base, nucleoside, and nucleotide aminohydrolase activity on pyrimidine bases and their nucleosides and nucleotides. Only adenosine aminohydrolase activity was demonstrated.
R J, Bauer, D M, Carlberg
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Characterization of bovine liver guanine aminohydrolase

International Journal of Biochemistry, 1981
Abstract 1. 1. The isoelectric points of bovine liver guanine aminohydrolase and xanthine oxidase are 4.90 and 6.25, respectively. 2. 2. The molecular weight of the guanine aminohydrolase is 95,000. 3. 3. The guanine aminohydrolase is formed from two subunits of identical molecular weight.
J M, Galilea, E I, Canela, J, Bozal
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On the regulatory properties of deoxycytidylate aminohydrolase

Biochemical and Biophysical Research Communications, 1964
Abstract In a previous paper we suggested the occurrence of at least one regulatory site ( Scarano et al., 1962 , Scarano et al., 1963 ) on dCMP aminohydrolase. The present paper reports further experiments that support this hypothesis.
E, Scarano, G, Geraci, M, Rossi
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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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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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A fluorimetric assay for guanine aminohydrolase

Analytical Biochemistry, 1974
Abstract A rapid, sensitive, and versatile assay for guanine aminohydrolase is described. It is based on the difference in native fluorescence of guanine, the substrate, and xanthine, the reaction product when excitation and emission wavelengths are 285 nm and 345 nm, respectively.
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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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Deoxycytidylate aminohydrolase during embryonic development of Rana esculenta

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1965
Abstract 1. The amount of deCMP-deaminase (deoxycytidylate aminohydrolase) per embryo has been determined in different stages of development of Rana esculenta. An increase in the content of enzyme per embryo was observed during development. The enzymic content increases approximately twice during the period from cleavage to the end of gastrulation ...
B, DEPETROCELLIS, P, GRANT, E, SCARANO
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