PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3466649-3	1987	At a ratio of one tetrathionate per mole of rhodanese, 100% of enzyme activity was lost in the sulfur-free E-form as compared with a 70% loss for the sulfur-containing ES-form of the enzyme.	Einsteinium	168-170	thiosulfate sulfurtransferase	Bos taurus	44-53	
11131146-5	2000	We have studied the unfolding and refolding of three rhodanese forms whose crystal structures are known: ES, containing the transferred sulfur as a persulfide; E, without the transferred sulfur, and carboxymethylated rhodanese (CMR), in which the active site was blocked by chemical modification.	Einsteinium	105-107	thiosulfate sulfurtransferase	Bos taurus	53-62	
3466649-8	1987	The substrate, thiosulfate, could reactivate the enzyme up to 70% in 1 h with ES as compared to 24 h with E. Tetrathionate modification of rhodanese could be correlated with the changes in intrinsic fluorescence and with the binding of the active site reporter 2-anilinonaphthalene-8-sulfonic acid (2,8-ANS).	Einsteinium	78-80	thiosulfate sulfurtransferase	Bos taurus	139-148	
6948580-3	1982	The effect with ES is fully reversible and almost completely so with E. Fluorescence depolarization sudies with thiosulfate sulfurtransferase labeled at a number of different sites with the fluorosphore dimethylaminonaphthalene show a sharp increase in the polarization starting at 27 degrees C when the temperature/viscosity ratio is varied with temperature and no transition when the ratio is varied with glycerol.	Einsteinium	16-18	thiosulfate sulfurtransferase	Bos taurus	112-141