Tocotrienols Inhibit Human Glutathione S-Transferase P1-1
نویسندگان
چکیده
منابع مشابه
Reversible conjugation of ethacrynic acid with glutathione and human glutathione S-transferase P1-1.
The reversibility of the conjugation reaction of the diuretic drug ethacrynic acid (EA), an alpha,beta-unsaturated ketone, with glutathione and glutathione S-transferase P1-1 (GST P1-1) has been studied. When the glutathione conjugate of EA was incubated with a 5-fold molar excess of N-acetyl-L-cysteine or GST P1-1, a time-dependent transfer of EA to N-acetyl-L-cysteine or GST P1-1 was observed...
متن کاملTocopherol esters inhibit human glutathione S-transferase omega.
Human glutathione S-transferase omega 1-1 (hGSTO1-1) is a newly identified member of the glutathione S-transferase (GST) family of genes, which also contains alpha, mu, pi, sigma, theta, and zeta members. hGSTO1-1 catalyzes the reduction of arsenate, monomethylarsenate (MMA(V)), and dimethylarsenate (DMA(V)) and exhibits thioltransferase and dehydroascorbate reductase activities. Recent evidenc...
متن کاملEstrogen receptor 1, glutathione S-transferase P1, glutathione S-transferase M1, and glutathione S-transferase T1 genes with dysmenorrhea in Korean female adolescents.
BACKGROUND Dysmenorrhea is the most common gynecologic complaint among adolescent females. We investigated the association between genetic polymorphisms and dysmenorrhea. METHODS A total of 202 postmenarcheal Korean female adolescents 16-17 yr old participated in this study. Genotyping for glutathione S-transferase mu 1 (GSTM1), glutathione S-transferase theta 1 (GSTT1), glutathione S-transfe...
متن کاملSite-directed Mutagenesis of Arginine 13 Residue in Human Glutathione S-Transferase P1-1
In order to study the role of residue in the active site of glutathione S-transferase (GST), Arg13 residue in human GST P1-1 was replaced with alanine, lysine and leucine by site-directed mutagenesis to obtain mutants R13A, R13K and R13L. These three mutant enzymes were expressed in Escherichia coli and purified to electrophoretic homogeneity by affinity chromatography on immobilized GSH. Mutat...
متن کاملGlutathione S-transferase P1 genotype and prognosis in Hodgkin's lymphoma.
PURPOSE Glutathione S-transferase P1 (GSTP1) is a member of the GST enzyme superfamily that is important for the detoxification of several cytotoxic drugs and their by-products. A single nucleotide polymorphism results in the substitution of isoleucine (Ile) to valine (Val) at codon 105, causing a metabolically less active variant of the enzyme. We assessed the impact of the GSTP1 codon 105 gen...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: IUBMB Life (International Union of Biochemistry and Molecular Biology: Life)
سال: 2002
ISSN: 1521-6543,1521-6551
DOI: 10.1080/15216540214315