Direct biosynthesis of the 29,30-bisnoramyrin system from 29,30-bisnor-2,3-oxidosqualene in pea seedlings

1968 ◽  
Vol 90 (18) ◽  
pp. 5045-5046 ◽  
Author(s):  
E. J. Corey ◽  
S. K. Gross
2020 ◽  
Vol 16 (4) ◽  
pp. 537-542
Author(s):  
Zhigacheva Irina ◽  
Volodkin Aleksandr ◽  
Rasulov Maksud

Background: One of the main sources of ROS in stress conditions is the mitochondria. Excessive generation of ROS leads to oxidation of thiol groups of proteins, peroxidation of membrane lipids and swelling of the mitochondria. In this regard, there is a need to search for preparationsadaptogens that increase the body's resistance to stress factors. Perhaps, antioxidants can serve as such adaptogens. This work aims at studying the effect of antioxidant; the potassium anphen in a wide range of concentrations on the functional state of 6 day etiolated pea seedlings mitochondria (Pisum sativum L). Methods: The functional state of mitochondria was studied per rates of mitochondria respiration, by the level of lipid peroxidation and study of fatty acid composition of mitochondrial membranes by chromatography technique. Results: Potassium anphen in concentrations of 10-5 - 10-8 M and 10-13-10-16 prevented the activation of LPO in the mitochondrial membranes of pea seedlings, increased the oxidation rates of NAD-dependent substrates and succinate in the respiratory chain of mitochondria that probably pointed to the anti-stress properties of the drug. Indeed, the treatment of pea seeds with the preparation in concentrations of 10-13 M prevented the inhibition of growth of seedlings in conditions of water deficiency. Conclusion: It is assumed that the dose dependence of the biological effects of potassium anphen and the manifestation of these effects in ultra-low concentrations are due to its ability in water solutions to form a hydrate containing molecular ensembles (structures).


2021 ◽  
pp. 1869415
Author(s):  
Andrey Khlopkov ◽  
Oksana Sherstneva ◽  
Maria Ladeynova ◽  
Marina Grinberg ◽  
Lyubov Yudina ◽  
...  

1961 ◽  
Vol 48 (3) ◽  
pp. 256-261 ◽  
Author(s):  
Betty F. Thomson ◽  
Pauline Monz Miller

2015 ◽  
Vol 22 (23) ◽  
pp. 19060-19068 ◽  
Author(s):  
Irina Shtangeeva ◽  
Matti Niemelä ◽  
Paavo Perämäki ◽  
Sergey Timofeev

Plant Science ◽  
1994 ◽  
Vol 99 (2) ◽  
pp. 135-140 ◽  
Author(s):  
Laura Marabini ◽  
Sonia Radice ◽  
Barbara Cipelletti ◽  
Enzo Chiesara

1999 ◽  
Vol 40 (3) ◽  
pp. 281-288
Author(s):  
T. Shimada ◽  
M. Miyao-Tokutomi ◽  
S. Tokutomi

1997 ◽  
Vol 43 (4) ◽  
pp. 51-54
Author(s):  
P. P. Golikov

The central link in the mechanism of action of glucocorticoids is specific cytoplasmic glucocorticoid receptors (GH). Their synthesis is programmed by 1 gene of chromosome 5 [44]. The direct biosynthesis of GR occurs in the endoplasmic reticulum of the cytoplasm [12]. In the cytoplasm, GRs bind to heat shock proteins (HSP, chaperone proteins) mol. mass of 50, 70, 90 kD [20, 59]. Like the mass of the GR – HSP complex is 300 kD [14]. In the absence of glucocorticoids, GRs are localized mainly in the cytoplasm [30, 63]. In 1 cell contains from 5000 to 100 000 specific GH. GRs have been found in many mammalian tissues [13], however, certain tissues do not contain GRs: the intermediate pituitary, Kupffer and endothelial cells of the liver, renal glomeruli, and proximal convoluted tubules [12, 31].


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