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Kinetic independence of the subunits of cytosolic glutathione transferase from the rat
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry, Biochemistry.
1985 (English)In: Biochemical Journal, ISSN 0264-6021, E-ISSN 1470-8728, Vol. 231, no 2, 263-267 p.Article in journal (Refereed) Published
Abstract [en]

The steady-state kinetics of the dimeric glutathione transferases deviate from Michaelis-Menten kinetics, but have hyperbolic binding isotherms for substrates and products of the enzymic reaction. The possibility of subunit interactions during catalysis as an explanation for the rate behaviour was investigated by use of rat isoenzymes composed of subunits 1, 2, 3 and 4, which have distinct substrate specificities. The kinetic parameter kcat./Km was determined with 1-chloro-2,4-dinitrobenzene, 4-hydroxyalk-2-enals, ethacrynic acid and trans-4-phenylbut-3-en-2-one as electrophilic substrates for six isoenzymes: rat glutathione transferases 1-1, 1-2, 2-2, 3-3, 3-4 and 4-4. It was found that the kcat./Km values for the heterodimeric transferases 1-2 and 3-4 could be predicted from the kcat./Km values of the corresponding homodimers. Likewise, the initial velocities determined with transferases 3-3, 3-4 and 4-4 at different degrees of saturation with glutathione and 1-chloro-2,4-dinitrobenzene demonstrated that the kinetic properties of the subunits are additive. These results show that the subunits of glutathione transferase are kinetically independent.

Place, publisher, year, edition, pages
1985. Vol. 231, no 2, 263-267 p.
National Category
Chemical Sciences
URN: urn:nbn:se:uu:diva-121138ISI: A1985ASU5800002PubMedID: 4062896OAI: oai:DiVA.org:uu-121138DiVA: diva2:343700
Available from: 2010-08-15 Created: 2010-03-18 Last updated: 2010-10-07Bibliographically approved

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