Alteration of enzyme activities and kinetic properties of GST and NQO1 with naturally occurring phenolic compounds

Date

2015-01-01

Author

KARAKURT, SERDAR
Sever, Melike
Celebioglu, Hasan Ufuk
Adalı, Orhan

Metadata

Show full item record

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Item Usage Stats

228
views

0
downloads

Objective: Glutathione S-transferase (GST) and NAD(P)H:quinine oxidoreductase 1 (NQO1) are the enzymes important in cytoprotection and bioactivation of chemicals. This study has addressed effects of polyphenolic compounds; ellagic acid, quercetin, naringenin, resveratrol, rutin and hesperidin on rabbit liver GST and NQO1 enzyme activities.

Subject Keywords

Clinical Biochemistry, Biochemistry, Molecular Biology, Biochemistry, medical

URI

https://hdl.handle.net/11511/40843

Journal

TURKISH JOURNAL OF BIOCHEMISTRY-TURK BIYOKIMYA DERGISI

DOI

https://doi.org/10.1515/tjb-2015-0010

Collections

Department of Biology, Article

Suggestions

OpenMETU
Core

Purification of glutathione S-transferases and genetic characterization of Zeta isozyme from Pinus brutia, Ten Öztetik, Elif; İşcan, Mesude; Department of Biochemistry (2005) Glutathione S-transferases (GST, EC2.5.1.18) are a family of multifunctional, dimeric enzymes that catalyse the nucleophilic attack of the tripeptide glutathione (?-L-glutamyl-L-cysteinyl-L-glycine) on lipophilic compounds with electrophilic centres. The primary function of GSTs is generally considered to be the detoxification of both endogenous and xenobiotic compounds. Cytosolic GSTs have been grouped into eleven distinct classes as: (A); Alpha, (M); Mu, (P); Pi, (S); Sigma, (T); Theta, (Z); Zeta, (F); Ph...
Investigation for natural extract inhibitors of bovine lens aldose reductase responsible for the formation of diabetis dependent cataract Onay, Melih; Çoruh, Nursen; Department of Biochemistry (2008) In the polyol pathway, Aldose reductase (AR) is an important enzyme in reduction of aldehydes and aldosugars to their suitable alcohols. AR, using NADPH as a coenzyme, has a molecular weight of 37 000 dalton. AR in its activated form, known to increase the sorbitol accumulation in lens, is responsible for the cataract formation in diabetis diseases. Therefore, the inhibition of aldose reductase is important to prevent the incedence of cataract formation in diabetus mellitus. In the treatment of diabetis dep...
Isolation and immunological characterization of theta class glutathione-s-transferase gstt2-2 from bovine liver İşgör, Sultan Belgin; Çoruh, Nursen; Department of Biochemistry (2004) The glutathione-S-transferases (GSTs) (EC.2.5.1.18) are enzymes that participate in cellular detoxification of endogenous as well as foreign electrophilic compounds, function in the cellular detoxification systems and are evolved to protect cells against reactive oxygen metabolites by conjugating the reactive molecules to the nucleophile scavenging tripeptide glutathione (GSH, ?-glu-cys-gly). The GSTs are found in all eukaryotes and prokaryotic systems, in the cytoplasm, on the microsomes, and in the mitoch...
AMINO-ACID SUBSTITUTIONS WITHIN THE ANALOGOUS NUCLEOTIDE-BINDING LOOP (P-LOOP) OF AMINOGLYCOSIDE 3'-PHOSPHOTRANSFERASE-II KOCABIVIK, S; PERLIN, MH (Elsevier BV, 1994-01-01) 1. Oligonucleotide-directed mutagenesis of APH(3')-II was used to investigate the functions of key amino acids in the P-loop analogous motif of the enzyme. 2. The mutations of Gly205 --> GIu, Gly210 --> Ala and Arg211 --> Pro considerably reduced the resistance of the resulting strains to KM and to related drugs, e.g. G418. 3. Similarly, enzyme activity in the crude extracts of these mutants was substantially reduced as well as the enzyme's affinity for Mg2+ ATP. 4. Alternatively substitutions at a highly c...
POSSIBLE INVOLVEMENT OF MANGANESE IN THE CATALYTIC MECHANISM OF BOVINE LIVER ARGINASE TURKOGLU, S; OZER, I (Elsevier BV, 1992-06-01) 1. Bovine liver arginase followed Michaelis-Menten kinetics in the pH range of 4.5-9.0. The variation of upsilon(i) pH implied that a basic group (pK(alpha) 8.7) functions at the catalytic site.

Citation Formats

S. KARAKURT, M. Sever, H. U. Celebioglu, and O. Adalı, “Alteration of enzyme activities and kinetic properties of GST and NQO1 with naturally occurring phenolic compounds,” TURKISH JOURNAL OF BIOCHEMISTRY-TURK BIYOKIMYA DERGISI, pp. 251–257, 2015, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/40843.