PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16668713-8	1992	The presence of DTT alone increases the size of the phosphoenolpyruvate carboxylase molecule as determined by light scattering.	Dithiothreitol	16-19	MLO-like protein 4	Zea mays	52-83	
24458697-2	1984	The inactivation by CuCl2 could be reversed by dithiothreitol, suggesting the involvement of vicinal dithiols in the inactivation process.Complete inactivation of phosphoenolpyruvate carboxylase was correlated with the incorporation of two mol ((3)H)N-ethylmaleimide per 100-kilodalton subunit.	Dithiothreitol	47-61	MLO-like protein 4	Zea mays	163-194	
16663773-1	1984	Incubation of purified phosphoenolpyruvate carboxylase from Zea mays L. leaves with dithiothreitol resulted in an almost 2-fold increase in the enzymic activity.	Dithiothreitol	84-98	MLO-like protein 4	Zea mays	23-54	
16663773-3	1984	The activation induced by dithiothreitol was reversed by diamide, an oxidant of vicinal dithiols, suggesting that the redox state of disulfide bonds of the enzyme may be important in the expression of the maximal catalytic activity.Titration of thiol groups before and after activation of maize phosphoenolpyruvate carboxylase by dithiothreitol shows an increase of the accessible groups from 8 to 12 suggesting that the reduction of two disulfide bonds accompanied the activation.	Dithiothreitol	26-40	MLO-like protein 4	Zea mays	295-326	
16663773-3	1984	The activation induced by dithiothreitol was reversed by diamide, an oxidant of vicinal dithiols, suggesting that the redox state of disulfide bonds of the enzyme may be important in the expression of the maximal catalytic activity.Titration of thiol groups before and after activation of maize phosphoenolpyruvate carboxylase by dithiothreitol shows an increase of the accessible groups from 8 to 12 suggesting that the reduction of two disulfide bonds accompanied the activation.	Dithiothreitol	330-344	MLO-like protein 4	Zea mays	295-326	
16663773-5	1984	It is concluded that the mechanism of phosphoenolpyruvate carboxylase activation by dithiothreitol involves the net reduction of two disulfide bonds in the enzyme.	Dithiothreitol	84-98	MLO-like protein 4	Zea mays	38-69	
11773521-3	2001	The purified PEPC-PK was readily inactivated under mild oxidative conditions, but the activity could be recovered by dithiothreitol (DTT).	Dithiothreitol	117-131	MLO-like protein 4	Zea mays	13-17	
11773521-3	2001	The purified PEPC-PK was readily inactivated under mild oxidative conditions, but the activity could be recovered by dithiothreitol (DTT).	Dithiothreitol	133-136	MLO-like protein 4	Zea mays	13-17