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Isolation and Characterization of Glutathione
S-Transferase Isozymes from Sorghum1
John W. Gronwald* and
Kathryn L. Plaisance
Plant Science Research Unit, Agricultural Research Service, United
States Department of Agriculture (J.W.G.), and Department of Agronomy
and Plant Genetics (K.L.P.), University of Minnesota, St. Paul,
Minnesota 55108
Two glutathione
S-transferase (GST) isozymes, A1/A1 and B1/B2, were
purified from etiolated,
O-1,3-dioxolan-2-yl-methyl-2,2,2,-trifluoro-4 -chloroacetophenone-oxime-treated sorghum (Sorghum bicolor L. Moench) shoots. GST A1/A1, a
constitutively expressed homodimer, had a subunit molecular mass of 26 kD and an isoelectric point of 4.9. GST A1/A1 exhibited high activity with 1-chloro-2, 4,dinitrobenzene (CDNB) but low activity with the
chloroacetanilide herbicide metolachlor. For GST A1/A1, the random,
rapid-equilibrium bireactant kinetic model provided a good description
of the kinetic data for the substrates CDNB and glutathione (GSH). GST
B1/B2 was a heterodimer with subunit molecular masses of 26 kD
(designated the B1 subunit) and 28 kD (designated the B2 subunit) and a
native isoelectric point of 4.8. GST B1/B2 exhibited low activity with
CDNB and high activity with metolachlor as the substrate. The kinetics
of GST B1/B2 activity with GSH and metolachlor fit a model describing a
multisite enzyme having two binding sites with different affinities for
these substrates. Both GST A1/A1 and GST B1/B2 exhibited
GSH-conjugating activity with ethacrynic acid and GSH peroxidase
activity with cumene hydroperoxide, 9-hydroperoxy-trans-10,cis-12-octadecadienoic
acid and
13-hydroperoxy-cis-9,trans-11-octadecadienoic acid. Both GST A1/A1 and GST B1/B2 are glycoproteins, as indicated by
their binding of concanavalin A. Polyclonal antibodies raised against
GST A1/A1 exhibited cross-reactivity with the B1 subunit of GST B1/B2.
Comparisons of the N-terminal amino acid sequences of the GST A1, B1,
and B2 subunits with other type I  -GSTs indicated a high degree of
homology with the maize GST I subunit and a sugarcane GST.
1
This work was a cooperative investigation of the
U.S. Department of Agriculture, Agricultural Research Service, and the
Minnesota Agricultural Experiment Station. This is Minnesota
Agricultural Experiment Station publication no. 97-1-13-0017.
*
Corresponding author; e-mail gronw001{at}maroon.tc.umn.edu; fax
1-612-649-5058.
Plant Physiol. (1998) 117: 877-892
Copyright Clearance Center: 0032-0889/98/117/0877/16
© 1998 American Society of Plant Physiologists
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