1,721,019 research outputs found
On the validity of continuous spectrophotometric assays for adenosine deaminase activity: A critical reappraisal
No full textKinetic investigations on adenosine deaminase from calf intestinal mucosa by spectrophotometric monitoring of the reaction at 264, 270, or 228 nm show that this method does not produce artifactual inhibition by substrate excess up to 0.7 mm concentration, when either adenosine or 2â2-deoxyadenosine are employed with calf adenosine deaminase. The evaluation of kinetic parameters for this system was carried out both by initial rate measurements and by numerical differentiation of time progress curves according to a recently published method (S. C. Koerber and A. L. Fink, 1987, Anal. Biochem. 165, 75-87). The following results were obtained by the latter method at pH 7.0 and 30°C: for the conversion of adenosine to inosine, kcat= 251 ± 15 s-1, KMs= 29.7 ± 2.8 Î1⁄4m, KMp= 613 ± 62 Î1⁄4m; for the conversion of 2â2-deoxyadenosine to 2â2-deoxyinosine, kcat= 283 ± 17 s-1, KMs= 22.4 ± 2.2 Î1⁄4m, KMp= 331 ± 35 Î1⁄4m. At 285 nm, a slight negative deviation from Beer's law was observed for adenosine at concentrations higher than 0.9 mm. No deviation was found for inosine up to 2.0 mm at the same wavelenth. © 1991
Comparing the photoresponses in different strains of Halobacterium salinarum: the puzzle is growing wilder
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Photoresponses in two strains of Halobacterium salinarum and current models for phototransduction
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The photosensory transduction in Halobacterium salinarium: An overview of behavioural and biophysical data
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Rapid-onset effect of visible light irradiation on the oxygen consumption rate in cultured cells
No full textThe effect of visible light irradiation on the oxygen consumption rate by cultured cells of different taxa
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