Quantification of human hepatic glutathione S-transferases
article
Human hepatic glutathione S-transferase (GST) subunits were characterized and quantified with the aid of a recently developed h.p.l.c. method. In 20 hepatic tissue specimens the absolute amounts of the basic Class Alpha subunits B1 and B2, the near-neutral Class Mu subunits μ and ψ and the acidic subunit π were determined. The average total amount of GST was 37 μg/mg of cytosolic protein, with the Class Alpha GST being the predominant class (84% of total GSTs), and π as the sole representative of the Class Pi GSTs present in the lowest concentration (4% of total GSTs). Large inter-individual differences were observed for all subunits, with variations up to 27-fold, depending on the subunit. For the Class Alpha GST-subunits B1 and B2, a biphasic ratio was observed. The genetic polymorphism of the subunits μ and ψ was confirmed by h.p.l.c. analysis, and correlated with the enzymic glutathione conjugation of trans-stilbene oxide and with Western blotting of cytosols, using a monoclonal anti-(Class Mu GST) antibody. Of the 20 livers examined, ten contained only μ, whereas the occurrence of ψ alone, and the combination of μ and ψ, were found in only one liver each.
TNO Identifier
48242
ISSN
0264-6021
Source
Biochemical Journal, 269(3), pp. 609-613.
Pages
609-613
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