1984
DOI: 10.1016/0003-2697(84)90657-2
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Detection of glutathione transferase activity on polyacrylamide gels

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Cited by 99 publications
(34 citation statements)
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“…For GST the gel was incubated for 10 min each in 0.1 MK-PO 4 buffer pH 6.5 and 0.1 MK-PO 4 buffer pH 6.5 containing 4.5 mM GSH, 1 mM CDNB and 1 mM NBT, followed by 0.1 M TrisHCl buffer pH 9.6 containing 3 mM phenazine methosulphate. Achromatic zones were discernable against dark blue background (Ricci et al 1984).…”
Section: In-gel Assays Of Antioxidant Enzymesmentioning
confidence: 99%
“…For GST the gel was incubated for 10 min each in 0.1 MK-PO 4 buffer pH 6.5 and 0.1 MK-PO 4 buffer pH 6.5 containing 4.5 mM GSH, 1 mM CDNB and 1 mM NBT, followed by 0.1 M TrisHCl buffer pH 9.6 containing 3 mM phenazine methosulphate. Achromatic zones were discernable against dark blue background (Ricci et al 1984).…”
Section: In-gel Assays Of Antioxidant Enzymesmentioning
confidence: 99%
“…The sites on the gel where the enzyme peroxidase was present were stained blue which after sometime turned brown confirming the presence of native peroxidase. Gels were stained for GST activity after native PAGE using the method of Ricci et al [23]. Blue insoluble formazan appeared on the gel surface in about 3 -5 min, except in the GST area.…”
Section: Activity Stainingmentioning
confidence: 99%
“…GST ISOENZYME ACTIVITY Equal amounts of protein were separated by 10% (w/v) native PAGE according to the method described by Laemmli (1970) and stained for GST activity according to Ricci et al (1984). Briefly, after electrophoresis, the gel was equilibrated in 0.1 M potassium phosphate buffer (pH 6.5) for 10 min and transferred to a reaction mixture containing 4.5 mM GSH, 1 mM CDNB and 1 mM nitroblue tetrazolium in 0.1 M potassium phosphate buffer (pH 6.5) at 37 o C for 10 min.…”
Section: Antioxidant Enzymes and Isoenzymesmentioning
confidence: 99%