PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6293543-6	1982	Several lanthanides as well as Mg(II) were found to displace Mn(II) from the strong site on bovine alpha-lactalbumin (as monitored by ESR) and to cause the identical fluorescence changes as found for Ca(II) and Mn(II) above.	Lanthanoid Series Elements	8-19	carbonic anhydrase 2	Bos taurus	200-206	
931985-2	1976	The substitution of lanthanide ions for Ca(II) in the Ca(II)-binding sites of prothrombin and the derivatives of prothrombin activation and in the metal-dependent conversion of prothrombin or prethrombin 1 to thrombin was studied at pH 6.8.	Lanthanoid Series Elements	20-30	carbonic anhydrase 2	Bos taurus	40-46	
931985-2	1976	The substitution of lanthanide ions for Ca(II) in the Ca(II)-binding sites of prothrombin and the derivatives of prothrombin activation and in the metal-dependent conversion of prothrombin or prethrombin 1 to thrombin was studied at pH 6.8.	Lanthanoid Series Elements	20-30	carbonic anhydrase 2	Bos taurus	54-60	
1167543-1	1975	The substitution of trivalent lanthanide ions for Ca(II) in the Ca(II)-DEPENDENT ACTIVATION OF BOVINE Factor X by the coagulant protein of Russell"s viper venom was studied at pH 6.8.	Lanthanoid Series Elements	30-40	carbonic anhydrase 2	Bos taurus	64-70	
1167543-9	1975	These data suggest that lanthanide ions complete with Ca(II) for the metal binding sites of Factor X and facilitate the formation of a nonproductive ternary complex of venom protein-Factor X-metal.	Lanthanoid Series Elements	24-34	carbonic anhydrase 2	Bos taurus	54-60