منابع مشابه
Kinetic studies on the regulation of rabbit liver pyruvate kinase.
Two kinetically distinct forms of pyruvate kinase (EC 2.7.1.40) were isolated from rabbit liver by using differential ammonium sulphate fractionation. The L or liver form, which is allosterically activated by fructose 1,6-diphosphate, was partially purified by DEAE-cellulose chromatography to give a maximum specific activity of 20 units/mg. The L form was allosterically activated by K(+) and op...
متن کاملKinetic and modelling studies of NAD+ and poly(ethylene glycol)-bound NAD+ in horse liver alcohol dehydrogenase.
Poly(ethylene glycol)-bound nicotinamide adenine dinucleotide (PEG-NAD+) has been successfully employed in the continuous production of L-amino acids from the corresponding alpha-keto acids by stereospecific reductive amination. Like many other dehydrogenases also horse liver alcohol dehydrogenase (HLADH) appears to be active with PEG-NAD+ as coenzyme, although the turnover number is three to f...
متن کاملKinetic studies with liver galactokinase.
1. Kinetic measurements of the forward reaction catalysed by ATP-galactose phosphotransferase were carried out with a purified preparation from pig liver. 2. The rate of reaction at pH7.8 is dependent on the concentration of MgATP(2-) rather than total ATP or magnesium chloride concentrations. 3. The effect of changes in pH on K(m) (galactose), K(m) (MgATP(2-)) and V(max.) was studied. 4. Of se...
متن کاملMechanism of malic enzyme from pigeon liver. Magnetic resonance and kinetic studies of the role of Mn2+.
As determined by EPR, malic enzyme from pigeon liver binds Mn2+ with a half-site stoichiometry of two tight binding sites (KD=6 to 10 mum) per enzyme tetramer and at two to four weak binding sites (KD=0.43 to 1.34 mM). The activation of malic enzyme by Mn2+ at high levels of L-malate shows biphasic kinetics yielding two activator constants for Mn2+. The dissociation constants of Mn2+ for both c...
متن کاملKinetic studies of dogfish liver glutamate dehydrogenase.
Initial-rate studies were made of the oxidation of L-glutamate by NAD+ and NADP+ catalysed by highly purified preparations of dogfish liver glutamate dehydrogenase. With NAD+ as coenzyme the kinetics show the same features of coenzyme activation as seen with the bovine liver enzyme [Engel & Dalziel (1969) Biochem. J. 115, 621--631]. With NADP+ as coenzyme, initial rates are much slower than wit...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1968
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1968.tb00390.x