PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6444600-10	1980	The ATPase reaction deviated from typical Michaelis-Menten kinetics in Tris-HCl buffer but not in Tris-bicarbonate.	Tris hydrochloride	71-79	dynein axonemal heavy chain 8	Homo sapiens	4-10	
215214-2	1978	Purified pig kidney ATPase was incubated in 30--160 mM Tris-HCl with various monovalent cations.	Tris hydrochloride	55-63	dynein axonemal heavy chain 8	Homo sapiens	20-26	
215214-16	1978	The total (Na+ + K+)-ATPase activity was markedly inhibited at high buffer concentrations (Tris-HCl, Imidazole-HCl and tetramethylammonium-HEPES gave similar results) in cases when either the concentration of Na+ or K+ (or both) was below saturation.	Tris hydrochloride	91-99	dynein axonemal heavy chain 8	Homo sapiens	21-27	
215214-19	1978	Under standard conditions (Tris-HCl + NaCl = 160 mM) the Na+-activation curve of Na+-ATPase had a steep rise between 0 and 2.5 mM, a fall between 2.5 and 20 mM and a further increase between 20 and 130 mM.	Tris hydrochloride	27-35	dynein axonemal heavy chain 8	Homo sapiens	85-91	
2141735-2	1990	Myofibrillar ATPase activity was inhibited by sodium hydroxymercuribenzoate (2.5 mM in 0.1 M Tris-HCl buffer, pH 7.2-7.5, 30 min) and successively reactivated by cysteine which was added to incubation solution (10 mM cysteine-HCl, 2.5 mM ATP-disodium salt, 50 mM potassium chloride and 27 mM calcium chloride in barbital buffer, pH 9.4, 35 min at 37 C).	Tris hydrochloride	93-101	dynein axonemal heavy chain 8	Homo sapiens	13-19