PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9723881-2	1998	A quantitative analysis of the interaction of metal ions with bovine Tg was conducted by fluorimetric titration of the protein with Tb3+ ions.	tb3+	132-136	thyroglobulin	Bos taurus	69-71	
9723881-4	1998	The fluorescence emission spectrum of Tg excited at 280 nm showed, upon addition of Tb3+ ions, a peak at 546 nm and a marked decrease at 335 nm, indicating an efficient Forster energy transfer between bound Tb3+ ions and closely located Tg intrinsic chromophores.	tb3+	84-88	thyroglobulin	Bos taurus	38-40	
9723881-4	1998	The fluorescence emission spectrum of Tg excited at 280 nm showed, upon addition of Tb3+ ions, a peak at 546 nm and a marked decrease at 335 nm, indicating an efficient Forster energy transfer between bound Tb3+ ions and closely located Tg intrinsic chromophores.	tb3+	84-88	thyroglobulin	Bos taurus	237-239	
9723881-4	1998	The fluorescence emission spectrum of Tg excited at 280 nm showed, upon addition of Tb3+ ions, a peak at 546 nm and a marked decrease at 335 nm, indicating an efficient Forster energy transfer between bound Tb3+ ions and closely located Tg intrinsic chromophores.	tb3+	207-211	thyroglobulin	Bos taurus	38-40	
9723881-5	1998	Titration of Tg with Tb3+ ions, carried out by monitoring the emitted fluorescence at 546 nm, indicated the presence of 13.15 metal binding sites per Tg molecule.	tb3+	21-25	thyroglobulin	Bos taurus	13-15	
9723881-5	1998	Titration of Tg with Tb3+ ions, carried out by monitoring the emitted fluorescence at 546 nm, indicated the presence of 13.15 metal binding sites per Tg molecule.	tb3+	21-25	thyroglobulin	Bos taurus	150-152