PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7648487-0	1995	Conformational changes of bovine bone osteonectin induced by interaction with calcium.	Calcium	78-85	secreted protein acidic and cysteine rich	Bos taurus	38-49	
3402455-5	1988	Thrombospondin-osteonectin complex formation was calcium-dependent as shown by a 50-80% inhibition in the presence of EDTA.	Calcium	49-56	secreted protein acidic and cysteine rich	Bos taurus	15-26	
7648487-1	1995	To clarify calcium-induced conformational changes in bovine bone osteonectin, the protein was labeled with fluorescein isothiocyanate (FITC) in the presence and absence of calcium.	Calcium	11-18	secreted protein acidic and cysteine rich	Bos taurus	65-76	
7648487-2	1995	By calcium titration using fluorescence spectrometry, it was demonstrated that FITC-osteonectin labeled in the presence of 2 mM CaCl2 showed a much higher affinity for calcium ions than did that labeled in the absence of calcium ions.	Calcium	3-10	secreted protein acidic and cysteine rich	Bos taurus	84-95	
7648487-2	1995	By calcium titration using fluorescence spectrometry, it was demonstrated that FITC-osteonectin labeled in the presence of 2 mM CaCl2 showed a much higher affinity for calcium ions than did that labeled in the absence of calcium ions.	Calcium	168-175	secreted protein acidic and cysteine rich	Bos taurus	84-95	
7648487-2	1995	By calcium titration using fluorescence spectrometry, it was demonstrated that FITC-osteonectin labeled in the presence of 2 mM CaCl2 showed a much higher affinity for calcium ions than did that labeled in the absence of calcium ions.	Calcium	168-175	secreted protein acidic and cysteine rich	Bos taurus	84-95	
7648487-5	1995	Furthermore, it was found that the efficacy of labeling in this specific binding site was three times higher in the FITC-osteonectin labeled in the presence of 2 mM CaCl2 than in that labeled in the absence of calcium.	Calcium	210-217	secreted protein acidic and cysteine rich	Bos taurus	121-132	
7648487-6	1995	The results indicate that in the presence of 2 mM CaCl2 the microenvironment around Lys174 of osteonectin was more open to modification than in the absence of calcium.	Calcium	159-166	secreted protein acidic and cysteine rich	Bos taurus	94-105	
2501009-7	1989	Osteonectin was purified from the calcium-induced precipitates from the EDTA extract of bovine bone.	Calcium	34-41	secreted protein acidic and cysteine rich	Bos taurus	0-11	
2501009-8	1989	By calcium titration using fluorescence spectrometry, the isolated osteonectin showed high affinity to calcium ions with an apparent dissociation constant (K0.5) of 8 x 10(-7) M. Thus, the use of calcium to separate bone proteins, especially osteonectin, was proved to be a useful technique.	Calcium	3-10	secreted protein acidic and cysteine rich	Bos taurus	67-78	
2501009-8	1989	By calcium titration using fluorescence spectrometry, the isolated osteonectin showed high affinity to calcium ions with an apparent dissociation constant (K0.5) of 8 x 10(-7) M. Thus, the use of calcium to separate bone proteins, especially osteonectin, was proved to be a useful technique.	Calcium	103-110	secreted protein acidic and cysteine rich	Bos taurus	67-78	
2501009-8	1989	By calcium titration using fluorescence spectrometry, the isolated osteonectin showed high affinity to calcium ions with an apparent dissociation constant (K0.5) of 8 x 10(-7) M. Thus, the use of calcium to separate bone proteins, especially osteonectin, was proved to be a useful technique.	Calcium	103-110	secreted protein acidic and cysteine rich	Bos taurus	67-78	
8245016-0	1993	Specific interaction of SPARC with endothelial cells is mediated through a carboxyl-terminal sequence containing a calcium-binding EF hand.	Calcium	115-122	secreted protein acidic and cysteine rich	Bos taurus	24-29	
2501009-9	1989	In addition, calcium-induced precipitation of osteonectin suggested a possible in vivo mechanism via which osteonectin might interact with calcium ions and participate in the initial immobilization of calcium to induce the nucleation of calcification in bone tissue.	Calcium	13-20	secreted protein acidic and cysteine rich	Bos taurus	46-57	
2501009-9	1989	In addition, calcium-induced precipitation of osteonectin suggested a possible in vivo mechanism via which osteonectin might interact with calcium ions and participate in the initial immobilization of calcium to induce the nucleation of calcification in bone tissue.	Calcium	13-20	secreted protein acidic and cysteine rich	Bos taurus	107-118	
2501009-9	1989	In addition, calcium-induced precipitation of osteonectin suggested a possible in vivo mechanism via which osteonectin might interact with calcium ions and participate in the initial immobilization of calcium to induce the nucleation of calcification in bone tissue.	Calcium	139-146	secreted protein acidic and cysteine rich	Bos taurus	46-57	
2501009-9	1989	In addition, calcium-induced precipitation of osteonectin suggested a possible in vivo mechanism via which osteonectin might interact with calcium ions and participate in the initial immobilization of calcium to induce the nucleation of calcification in bone tissue.	Calcium	139-146	secreted protein acidic and cysteine rich	Bos taurus	107-118	
2501009-9	1989	In addition, calcium-induced precipitation of osteonectin suggested a possible in vivo mechanism via which osteonectin might interact with calcium ions and participate in the initial immobilization of calcium to induce the nucleation of calcification in bone tissue.	Calcium	139-146	secreted protein acidic and cysteine rich	Bos taurus	46-57	
2501009-9	1989	In addition, calcium-induced precipitation of osteonectin suggested a possible in vivo mechanism via which osteonectin might interact with calcium ions and participate in the initial immobilization of calcium to induce the nucleation of calcification in bone tissue.	Calcium	139-146	secreted protein acidic and cysteine rich	Bos taurus	107-118