PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8570639-4	1996	Although the B2 site that preferentially binds purines on the 3" side of B1 is also weak, its associated phosphate subsites make substantial contributions: both 3",5"-ADP and 5"-ADP have Ki values 6-fold lower than for 5"-AMP, and adding a 3"-phosphate to the substrate CpA increases Kcat/Km by 9-fold.	Phosphates	105-114	carboxypeptidase A1	Homo sapiens	270-273	
9352079-1	1997	In this study we investigated the contribution of pH, phosphate anions and salt concentration to the catalytic and structural thermostability of the carboxypeptidase A (CPA).	Phosphates	54-63	carboxypeptidase A1	Homo sapiens	149-167	
9352079-1	1997	In this study we investigated the contribution of pH, phosphate anions and salt concentration to the catalytic and structural thermostability of the carboxypeptidase A (CPA).	Phosphates	54-63	carboxypeptidase A1	Homo sapiens	169-172	
9352079-2	1997	The concentration of 75-100 mM phosphate as well as neutral pH values were found to be optimal for stabilizing CPA at high temperatures.	Phosphates	31-40	carboxypeptidase A1	Homo sapiens	111-114	
9352079-4	1997	The experimental results and theoretical analysis suggested that the main contribution to heat stabilization of CPA is related to intramolecular electrostatic interactions and Arginine and/or Lysine are the putative groups able to bind phosphate and stabilize the enzyme molecule against thermal denaturation.	Phosphates	236-245	carboxypeptidase A1	Homo sapiens	112-115	
3718539-3	1986	The inhibitory effect of phosphate ions upon this activity of CPB (but not CPA) suggests that CPA may be responsible for the formation of free phenylalanine seen upon degradation of kinins in plasma or serum.	Phosphates	25-34	carboxypeptidase A1	Homo sapiens	94-97