Results 101 to 110 of about 1,424 (153)

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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Abstract 5649: Human Alanine: Glyoxylate Aminotransferase 2 Lowers ADMA and Protects From ADMA-induced Impairment in Nitric Oxide Production

Circulation, 2009
Elevated blood concentrations of asymmetric dimethylarginine (ADMA), an endogenous inhibitor of nitric oxide (NO) synthase, are found in association with diabetes, hypertension, congestive heart failure and atherosclerosis.
R. Rodionov, D. Murry, S. Lentz
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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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Degradation of Atrazine to Cyanuric Acid by an Encapsulated Enzyme Cascade

Catalysts
Atrazine (2-chloro-4-ethylamino-6-isopropylamino-s-triazine CAS: 1912-24-9) is a widely used herbicide that has been connected to a variety of negative human health and environmental effects. Various bacterial strains utilize a six-step enzyme cascade to
Maya Mowery-Evans, Emma Benzie, Noha Alansari, Michael J Melville, Dylan Domaille, Richard C. Holz   +5 more
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In vitro characterization of the ergothioneine oxidative catabolic pathway in Actinoplanes missouriensis ATCC 14538.

Biochemical and Biophysical Research Communications - BBRC
l-ergothioneine is a naturally occurring histidine thio-derivative produced by certain bacterial and fungal species. Plants acquire ergothioneine from soil, while animals ingest it through their diets.
Qiuni Long, Hua Huang, Xinshuai Zhang
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