Purification and characterization of aldose reductase from jerboa (Jaculus orientalis) and evaluation of its inhibitory activity by Euphorbia regis-jubae (Webb & Berth) extracts.
作者： Fouzia Hmimid , Noureddine Bourhim , Ahmed Errami , Fatima Azzahra Lahlou , Ismail Guenaou
DOI: 10.1016/J.CBPC.2021.109001
关键词: White adipose tissue 、 High-performance liquid chromatography 、 Jaculus orientalis 、 Enzyme assay 、 Catechin 、 Aldose reductase 、 Euphorbia 、 Chromatography 、 Enzyme 、 Chemistry
摘要: Abstract This study aimed, for the first time, to assess purification of aldose reductase (AR) in Jaculus orientalis (Dipodidae family) kidney and evaluate vitro inhibitory (ARI) effects Euphorbia regis-jubae (Euphorbiaceae aqueous hydroethanolic extracts. Initial screening assay enzymatic AR activity different jerboa states (euthermic, prehibernating hibernating) tissues (brain, brown adipose tissue, liver kidneys) was assessed. Then, has been purified homogeneity from kidneys jerboas by a series chromatographic technics. Furthermore, silico ARI E. (Webb & Berth) extracts, characterized hight performance liquid chromatography (HPLC) on enzyme were evaluated. Our results showed that highest detected kidneys, followed white tissue lungs pre-hibernating jerboa. The during state with factor 53.4-fold yield about 6%. is monomeric, active D(+)-glyceraldehyde substrate disodium phosphate buffer. pH temperature determined be 6.5–7.5 35 °C, respectively. Results strongest both extract (IC50 = 96.45 μg/mL) 140 μg/mL). Molecular docking indicated catechin might main component extracts inhibited AR. provides new evidence effect Berth), which may related its phenolic constituents.
sci-hub.st 参考文章(44)
Toshiyuki SUZUKI, Hiroshi ONISHI, Purification and Properties of Polyol: NADP Oxidoreductase from Pichia quercuum Agricultural and biological chemistry. ,vol. 39, pp. 2389- 2397 ,(1975) , 10.1271/BBB1961.39.2389
Nobuhisa Iwata, Norihisa Inazu, Tetsuo Satoh, None, The purification and properties of aldose reductase from rat ovary Archives of Biochemistry and Biophysics. ,vol. 282, pp. 70- 77 ,(1990) , 10.1016/0003-9861(90)90088-G
R.N. Gacche, N.A. Dhole, Profile of aldose reductase inhibition, anti-cataract and free radical scavenging activity of selected medicinal plants: An attempt to standardize the botanicals for amelioration of diabetes complications Food and Chemical Toxicology. ,vol. 49, pp. 1806- 1813 ,(2011) , 10.1016/J.FCT.2011.04.032
Ballabh Das, Satish K. Srivastava, Purification and properties of aldose reductase and aldehyde reductase II from human erythrocyte Archives of Biochemistry and Biophysics. ,vol. 238, pp. 670- 679 ,(1985) , 10.1016/0003-9861(85)90213-9
S.J Semple, G.D Reynolds, M.C O'Leary, R.L.P Flower, Screening of Australian medicinal plants for antiviral activity. Journal of Ethnopharmacology. ,vol. 60, pp. 163- 172 ,(1998) , 10.1016/S0378-8741(97)00152-9
Dik-Lung Ma, Daniel Shiu-Hin Chan, Chung-Hang Leung, Molecular docking for virtual screening of natural product databases Chemical Science. ,vol. 2, pp. 1656- 1665 ,(2011) , 10.1039/C1SC00152C
S Bani, A Kaul, B.S Jaggi, K.A Suri, O.P Suri, O.P Sharma, Anti-inflammatory activity of the hydrosoluble fraction of Euphorbia royleana latex Fitoterapia. ,vol. 71, pp. 655- 662 ,(2000) , 10.1016/S0367-326X(00)00225-2
L. Tona, K. Kambu, N. Ngimbi, K. Mesia, O. Penge, M. Lusakibanza, K. Cimanga, T. De Bruyne, S. Apers, J. Totte, L. Pieters, A.J. Vlietinck, Antiamoebic and spasmolytic activities of extracts from some antidiarrhoeal traditional preparations used in Kinshasa, Congo. Phytomedicine. ,vol. 7, pp. 31- 38 ,(2000) , 10.1016/S0944-7113(00)80019-7
S. Hayman, M.F. Lou, L.O. Merola, J.H. Kinoshita, Aldose reductase activity in the lens and other tissues Biochimica et Biophysica Acta. ,vol. 128, pp. 474- 482 ,(1966) , 10.1016/0926-6593(66)90008-7
Rex S. Clements, Albert I. Winegrad, Purification of alditol:NADP oxidoreductase from human placenta Biochemical and Biophysical Research Communications. ,vol. 47, pp. 1473- 1479 ,(1972) , 10.1016/0006-291X(72)90238-0