Reductive light activation of enzyme activity

2000 ◽  
Vol 110 (3) ◽  
pp. 295-295
Author(s):  
Louise Anderson ◽  
Per Gardestrom
Keyword(s):  
Enzyme Activity ◽  
Light Activation

scholarly journals Light activation of fructose bisphosphatase in photosynthetically competent pea chloroplasts

1981 ◽  
Vol 200 (2) ◽  
pp. 357-363 ◽  
Author(s):  
S A Charles ◽  
B Halliwell
Keyword(s):  
Enzyme Activity ◽  
Steady State ◽  
Co2 Fixation ◽  
Enzyme Activation ◽  
Dihydroxyacetone Phosphate ◽  
Fructose Bisphosphatase ◽  
Light Activation ◽  
Role Of Light ◽  
Assay Conditions

The fructose bisphosphatase (EC 3.1.3.11) activity of type A chloroplasts isolated from young (9-day-old) pea (Pisum sativum var. Progress no. 9) plants, assayed at physiological pH, substrate and Mg2+ concentrations, increased rapidly on illumination. The enzyme activity detected was more than sufficient to account for observed rates of Co2 fixation both during the induction period and during steady-state CO2 fixation, whether or not dihydroxyacetone phosphate had been added to the preparation. Omission of catalase from the suspension medium had no effect. On switching off the light, CO2 fixation by the chloroplasts ceased at once, yet fructose bisphosphatase activity decreased much more slowly. Changes in enzyme activity were much less marked if assays were conducted at 3 mM substrate and 10 mM-Mg2+. Chloroplasts from older (13--20-day-old) peas only fixed CO2 rapidly if catalase was present in the assay medium. The fructose bisphosphatase activity detected under physiological assay conditions was again more than sufficient to account for observed rates of Co2 fixation. In the presence of added dihydroxyacetone phosphate, however, the rate of Co2 fixation appeared to be determined by the rate of light activation of fructose bisphosphatase. In general, the rates of Co2 fixation and enzyme activation, and the final enzyme activity achieved, decreased markedly with increasing age of the plants. The role of light activation of fructose bisphosphatase as a means of controlling the rate of CO2 fixation in pea chloroplasts is discussed.

Reductive light activation of enzyme activity

2008 ◽  
Vol 110 (3) ◽  
pp. 295-295
Author(s):  
Louise Anderson ◽  
Per Gardeström
Keyword(s):  
Enzyme Activity ◽  
Light Activation

Morphological and biochemical analyses of changes in rat hepatocytes related to wine and ethanol consumption

1984 ◽  
Vol 42 ◽  
pp. 232-233
Author(s):  
S.M. Geyer ◽  
C.L. Mendenhall ◽  
J.T. Hung ◽  
E.L. Cardell ◽  
R.L. Drake ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Enzyme Activity ◽  
Malic Enzyme ◽  
Smooth Endoplasmic Reticulum ◽  
Rat Hepatocytes ◽  
Mature Male ◽  
Treatment Groups ◽  
Malic Enzyme Activity ◽  
Biochemical Analyses

Thirty-three mature male Holtzman rats were randomly placed in 3 treatment groups: Controls (C); Ethanolics (E); and Wine drinkers (W). The animals were fed synthetic diets (Lieber type) with ethanol or wine substituted isocalorically for carbohydrates in the diet of E and W groups, respectively. W received a volume of wine which provided the same gram quantity of alcohol consumed by E. The animals were sacrificed by decapitation after 6 weeks and the livers processed for quantitative triglycerides (T3), proteins, malic enzyme activity (MEA), light microscopy (LM) and electron microscopy (EM). Morphometric analysis of randomly selected LM and EM micrographs was performed to determine organellar changes in centrilobular (CV) and periportal (PV) regions of the liver. This analysis (Table 1) showed that hepatocytes from E were larger than those in C and W groups. Smooth endoplasmic reticulum decreased in E and increased in W compared to C values.

Light-activation of NADP-malate dehydrogenase: A highly controlled process for an optimized function

2000 ◽  
Vol 110 (3) ◽  
pp. 322-329 ◽  
Author(s):  
M. Miginiac-Maslow ◽  
K. Johansson ◽  
E. Ruelland ◽  
E. Issakidis-Bourguet ◽  
I. Schepens ◽  
...  
Keyword(s):  
Malate Dehydrogenase ◽  
Light Activation

HYDRATION AND ENZYME ACTIVITY

1984 ◽  
Vol 45 (C7) ◽  
pp. C7-249-C7-253
Author(s):  
P. L. Poole
Keyword(s):  
Enzyme Activity

Evaluation of Azadirachtin on Arthrospira plantensis Gomont growth parameters and antioxidant enzymes

2020 ◽  
Vol 56 ◽  
pp. 8
Author(s):  
Hatice Tunca ◽  
Ali Doğru ◽  
Feray Köçkar ◽  
Burçin Önem ◽  
Tuğba Ongun Sevindik
Keyword(s):  
Enzyme Activity ◽  
Growth Parameters ◽  
Arthrospira Platensis ◽  
Proline Content ◽  
Enzyme Analysis ◽  
Free Proline ◽  
Sod Activity ◽  
Pesticide Pollution ◽  
Antioxidant Parameters ◽  
Mda Content

Azadirachtin (Aza) used as insecticide due to inhibiting growth of insects and preventing them from feeding on plants. To understand the effects of contamination of this insecticide on phototrophs, and to determine the responses of these organisms against these insecticides are extremely important in understanding how the ecosystem is affected. In this study, chlorophyll-a amount, OD 560 and antioxidant parameters (total SOD, APX, GR, Proline, MDA and H2O2) were determined in order to understand the effect of Aza on Arthrospira platensis Gomont. Aza was applied between 0–20 μg mL−1 concentrations for 7 days in the study. Enzyme analysis was conducted at the end of the 7th day. There was a statistically significant decrease in the absorbance of OD560 and the chlorophyll-a content in A. platensis cultures exposed to the Aza (0–20 μg mL−1) during 7 days due to the increase in pesticide levels. SOD activity decreased at 8, 16 and 20 μg mL−1 concentrations; GR enzyme activity showed a significant decrease compared to the control at a concentration of 20 μg mL−1. APX activity did not change significantly compared to control. The MDA content increased significantly at 16 and 20 μg mL−1 concentrations. The H2O2 content significantly increased at 12, 16 and 20 μg mL−1 concentrations (p < 0.05) while the free proline content decreased at 4 μg mL−1 concentration (p < 0.05). As a result, regarding the Aza concentrations used in this study may be a step to prevent pesticide pollution in the environment.

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