Title : Class sigma glutathione transferase unfolds via a dimeric and a monomeric intermediate: impact of subunit interface on conformational stability in the superfamily.

Pub. Date : 1998 Nov 3

PMID : 9799517






1 Functional Relationships(s)
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1 Solvent-induced equilibrium unfolding of a homodimeric class sigma glutathione transferase (GSTS1-1, EC 2.5.1.18) was characterized by tryptophan fluorescence, anisotropy, enzyme activity, 8-anilino-1-naphthalenesulfonate (ANS) binding, and circular dichroism. 8-anilino-1-naphthalenesulfonic acid hematopoietic prostaglandin D synthase Homo sapiens