Bitki kökenli ekstrelerin sığır lens aldoz redüktaz enzimi üzerine inhibitör etkileri


Tezin Türü: Yüksek Lisans

Tezin Yürütüldüğü Kurum: Orta Doğu Teknik Üniversitesi, Türkiye

Tezin Onay Tarihi: 2004

Tezin Dili: İngilizce

Öğrenci: Selin Zaimoğlu

Danışman: NURSEN ÇORUH

Özet:

Aldose reductase, E.C.1.1.1.21, catalyzes the reduction of different types of aldehydes to their corresponding alcohols, and especially reduces various aldo-sugars using NADPH as the coenzyme. Under hyperglycemic conditions aldose reductase is involved in the development of diabetic complications. As a result, interest has been placed over the years on the development of potent aldose reductase inhibitors for possible use in the therapy of these severe diabetic complications. In this study, aldose reductase was isolated from bovine lens by differential centrifugation and ammonium sulfate precipitation. The conditions for the enzyme assay; such as substrate (DL-Glyceraldehyde) and coenzyme (NADPH) concentration, protein amount, effect of sulfate ions, temperature and pH on the enzyme activity were optimized. The inhibitory effects of Punica granatum, Spinacia olaeracea, Allium cepa Allium porrum, Malus flouribunda, Malus domestica extracts were tested on crude bovine lens aldose reductase. Four different types of organic fractions from each crude plant extract were obtained by solvent fractionation. The inhibitory activity of these organic fractions was calculated considering the aldose reductase activity without extracts as 100 %. All six plants were found to inhibit aldose reductase activity to different extent. Among these fractions obtained as; petroleum ether, diethyl ether, ethyl acetate, and n-butanol. Highest inhibitory activity was found for the ethyl acetate fraction. The IC50 values of ethyl acetate fractions of all these plants was calculated as, 25.46 æg/ml, 20.5 æg/ml, 18.5 æg/ml, 12.32 æg/ml, 6.45 æg/ml, 5.4 æg/ml, for Allium porrum, Malus domestica, Spinacia olaeracea, Malus floribunda Allium cepa, Punica granatum respectively.