PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2848987-3	1988	In contrast, Zn2+ inhibited the interaction of 2-hydroxyestradiol with microsomal protein as measured by the release of 3H from C-4 of the labeled steroids but did not influence 2-hydroxylation, except at high concentration.	2-hydroxyestradiol	47-65	complement C4A	Rattus norvegicus	128-131	
2847784-3	1988	The further metabolism of 2-hydroxyestradiol involves activation of the steroid at C-4 and, to a much lesser extent at C-1, by a cytochrome P-450 mediated reaction as indicated by the effects of NADPH, spermine, SKF-525A, and CO in the microsomal system.	2-hydroxyestradiol	26-44	complement C4A	Rattus norvegicus	83-86	
2847784-4	1988	Glutathione promoted the loss of 3H from C-4 of either estradiol or 2-hydroxyestradiol but had less effect on this reaction at C-1 and inhibited it at C-6,7.	2-hydroxyestradiol	68-86	complement C4A	Rattus norvegicus	41-44	
3018374-2	1986	A ratio of about 3.5:1 for the C-4 and C-1 thioether conjugates of 2-OHE2 was observed.	2-hydroxyestradiol	67-73	complement C4A	Rattus norvegicus	31-34