Results 131 to 140 of about 2,006 (160)
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Trichomonas vaginalis:Expression and Characterisation of RecombinantS-Adenosylhomocysteinase
Experimental Parasitology, 1998The gene encoding S-adenosylhomocysteinase activity (S-adenosylhomocysteine hydrolase, SAHH; EC 3.3.1.1) in Trichomonas vaginalis has been expressed in Escherichia coli to facilitate the characterisation of the enzyme. Expression of this gene using the pQE-30 (6xHis N-terminal tag) expression system (QIAGEN) has enabled the one-step purification of 6 ...
Aldo S Bagnara, M R Edwards
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BBA - Proteins and Proteomics, 1984
The spectral changes observed on interaction of S-adenosylhomocysteinase with adenine and cordycepin are approximated by the addition of dimethylsulfoxide to the aqueous solutions of these compounds, but not by protonation of the compounds. Although adenosine when bound to the enzyme undergoes partial reactions, it gives a spectral change similar to ...
Tomoharu Gomi, T Gomi, Motoji Fujioka
exaly +3 more sources
The spectral changes observed on interaction of S-adenosylhomocysteinase with adenine and cordycepin are approximated by the addition of dimethylsulfoxide to the aqueous solutions of these compounds, but not by protonation of the compounds. Although adenosine when bound to the enzyme undergoes partial reactions, it gives a spectral change similar to ...
Tomoharu Gomi, T Gomi, Motoji Fujioka
exaly +3 more sources
Rat liver S-adenosylhomocysteinase. Spectrophotometric study of coenzyme binding
BBA - Proteins and Proteomics, 1989Rat liver S-adenosylhomocysteinase, a homotetramer, was resolved by treatment with acid ammonium sulfate into apoenzyme and NAD. The apoenzyme thus prepared retained a tetrameric structure but differed in the mobility on nondenaturing polyacrylamide gel electrophoresis. The inactive apoenzyme was reactivated upon incubation with NAD. The restoration of
Yoshimi Takata, Tomoharu Gomi, T Gomi
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Adenosylhomocysteinase:Adenosine complex
Biochemical and Biophysical Research Communications, 1978Adenosylhomocysteinase from yellow lupin seeds forms a specific complex with adenosine. The complex can be isolated either by nonequilibrium or equilibrium gel filtration. It is also adsorbed on nitrocellulose disks. Dissociation constant of the complex determined by nitrocellulose filter assay is 5 × 10−8M.
Hieronim Jakubowski +2 more
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Inactivation of rat liver S-adenosylhomocysteinase by iodoacetamide
Biochemistry, 1982S-Adenosylhomocysteine (EC 3.3.1.1) from rat liver is inactivated by iodoacetamide following pseudo-first-order reaction kinetics. The apparent first-order rate constant for inactivation is proportional to the concentration of the modifier, and a value of 7.55 M-1 min-1 is obtained for the second-order rate constant at pH 9.06 and 25 degrees C.
Tomoharu Gomi, T Gomi, Motoji Fujioka
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Biochemistry, 1982
S-Adenosylhomocysteinase (SAHase), a tetrameric enzyme, is inactivated by 2'-deoxyadenosine (2'dAdo) in a time-dependent process [Hirshfield, M. S. (1979) J. Biol. Chem. 254, 22-25]. It has been proposed that inactivation involves oxidation of 2'dAdo at C-3' by enzyme-bound nicotinamide adenine dinucleotide (NAD), subsequent proton abstraction at C-2',
R H Abeles, Robert H Abeles
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S-Adenosylhomocysteinase (SAHase), a tetrameric enzyme, is inactivated by 2'-deoxyadenosine (2'dAdo) in a time-dependent process [Hirshfield, M. S. (1979) J. Biol. Chem. 254, 22-25]. It has been proposed that inactivation involves oxidation of 2'dAdo at C-3' by enzyme-bound nicotinamide adenine dinucleotide (NAD), subsequent proton abstraction at C-2',
R H Abeles, Robert H Abeles
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5'-[p-(Fluorosulfonyl)benzoyl]adenosine-mediated inactivation of S-adenosylhomocysteinase
Biochemistry, 1984Rat liver S-adenosylhomocysteinase (EC 3.3.1.1) is inactivated by 5'-[p-(fluorosulfonyl)benzoyl]adenosine following pseudo-first-order kinetics. A plot of the apparent first-order rate constant for inactivation vs. the 5'-[p-(fluorosulfonyl)benzoyl]adenosine concentration exhibits a hyperbolic curve indicative of the formation of a reversible enzyme ...
Yoshimi Takata, Motoji Fujioka
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Cyclic AMP-adenosine binding protein/S-adenosylhomocysteinase from mouse liver
Biochimica Et Biophysica Acta - General Subjects, 19791. Adenosine bound to the cyclic AMP-adenosine binding protein/S-adenosylhomocysteinase from mouse liver was partly converted to a product which was identified as adenine in four chromatographic systems. Ribose was formed in equivalent amounts. 2. The time course of the reaction was characterized by an initial burst phase lasting for less than one ...
Per Magne Ueland
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Planta, 1978
The activities of adenosylhomocysteinase (EC 3.3.1.1) and adenosine nucleosidase (EC 3.2.2.7) were assayed in extracts from yellow lupin (Lupinus luteus L.) cotyledons at different stages of seed formation and seedling development. Adenosylhomocysteinase activity was demonstrated in all the cotyledon extracts examined. Its lowest level was found in the
A Guranowski
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The activities of adenosylhomocysteinase (EC 3.3.1.1) and adenosine nucleosidase (EC 3.2.2.7) were assayed in extracts from yellow lupin (Lupinus luteus L.) cotyledons at different stages of seed formation and seedling development. Adenosylhomocysteinase activity was demonstrated in all the cotyledon extracts examined. Its lowest level was found in the
A Guranowski
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Biochemistry, 1986
Homogeneous S-adenosylhomocysteinase (AdoHcyase) from rat liver is a tetrameric enzyme that contains four molecules of tightly bound NAD per mole of enzyme. We report here that incubation of the rat liver enzyme with ATP, Mg2+, and KCl leads to conversion of the active enzyme to an inactive form with release of all enzyme-bound NAD which can be ...
Argante Bozzi +2 more
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Homogeneous S-adenosylhomocysteinase (AdoHcyase) from rat liver is a tetrameric enzyme that contains four molecules of tightly bound NAD per mole of enzyme. We report here that incubation of the rat liver enzyme with ATP, Mg2+, and KCl leads to conversion of the active enzyme to an inactive form with release of all enzyme-bound NAD which can be ...
Argante Bozzi +2 more
exaly +3 more sources