منابع مشابه
The kinetics of alkaline phosphatase.
The repressible alkaline phosphatase of Escherichia coli (orthophosphoric monoester phosphohydrolase, EC 3.1.3.1) promises to play a role in biochemical genetics comparable to that played by fl-galactosidase (l-5). It is also being used increasingly for class experiments. The evaluation of the important characteristic kinetic constants for this enzyme, however, poses certain technical difficult...
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Members of the macrolide class of antibiotics inhibit peptide elongation on the ribosome by binding close to the peptidyltransferase center and blocking the peptide exit tunnel in the large ribosomal subunit. We have studied the modes of action of the macrolides josamycin, with a 16-membered lactone ring, and erythromycin, with a 14-membered lactone ring, in a cell-free mRNA translation system ...
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The mechanism of activation of the phosphoglucomutase reaction by the coenzyme, cu-glucose 1,6-diphosphate, was studied by Leloir et al. (1)) Sutherland et al. (2)) and Jagannathan and Luck (3). In 1954, Najjar and Pullman (4) showed that the active, phosphorylated form of the enzyme interacted with glucose l-phosphate to form the coenzyme and the inactive, dephosphorylated enzyme, and that the...
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The kinetic study of the condensation reaction between phloroglucinol and acetone was investigated at 30, 35, 40 and 45±0.05 °C in 100% methanol. The hydrochloric acid concentrations used were 0.0261, 0.0364, 0.0577 and 0.0728 M. The reaction was investigated with and without a promoter, thioglycollic acid (TGA), and taking into account the functionality (h<e...
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The reaction kinetics of the isomerization 3,4-dichlorobutene-1 to 1,4-dichlorobutene-2 was investigated by using gas-liquid chromatography method in the presence of Fe2O3/MgO as solid catalyst in the temperature range 25-55°C. Fe2O3/MgO has been prepared by the support saturation method, tested in the isomerization of 3, 4-dichlorobutene-1 into 1, 4-dichlorobutene-2. This catalyst shows a high...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1952
ISSN: 0306-3283
DOI: 10.1042/bj0500378