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J. Biol. Chem., Vol. 259, Issue 15, 9345-9347, Aug, 1984
GF Seelig, RP Simondsen and A Meister
gamma-Glutamylcysteine synthetase (rat kidney; Mr approximately 104,000) is
composed of 2 nonidentical subunits. In the present work, a procedure was
developed for the reversible dissociation of the enzyme into its subunits
(Mr = 73,000 and 27,700) under nondenaturing conditions. Students in which
gel electrophoresis was used, in conjunction with an enzyme activity stain
and elution and re- electrophoresis of protein bands, showed that the heavy
subunit contains all of the structural requirements for enzymatic activity
and also for feedback inhibition of the enzyme activity by glutathione. The
light subunit, which may be formed from a precursor protein, has a
significantly lower content of Trp, Phe, Tyr, Val, and Ala residues than
the heavy subunit, while its content of Lys, His, Met, and Asx residues is
higher.
Reversible dissociation of gamma-glutamylcysteine synthetase into two subunits
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