PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9659395-0	1998	X-ray studies on cross-linked lysozyme crystals in acetonitrile-water mixture.	acetonitrile	51-63	lysozyme	Homo sapiens	30-38	
11217018-6	2001	The displacer could be removed quantitatively from the protein fractions by thermal precipitation at 48 degrees C. Co-precipitation of lysozyme with the displacer was minimal in the presence of 3% (v/v) acetonitrile, while the lysozyme enzymatic activity in the supernatant was completely retained.	acetonitrile	203-215	lysozyme	Homo sapiens	135-143	
10631479-0	2000	On the stabilizing action of protein denaturants: acetonitrile effect on stability of lysozyme in aqueous solutions.	acetonitrile	50-62	lysozyme	Homo sapiens	86-94	
10631479-1	2000	Stability of hen lysozyme in the presence of acetonitrile (MeCN) at different pH values of the medium was studied by scanning microcalorimetry with a special emphasis on determination of reliable values of the denaturational heat capacity change.	acetonitrile	45-57	lysozyme	Homo sapiens	17-25	
10631479-1	2000	Stability of hen lysozyme in the presence of acetonitrile (MeCN) at different pH values of the medium was studied by scanning microcalorimetry with a special emphasis on determination of reliable values of the denaturational heat capacity change.	acetonitrile	59-63	lysozyme	Homo sapiens	17-25	
10631479-7	2000	At the higher MeCN content this dependence decreases until, at 0.06 mole fractions of MeCN, the difference in the preferential solvation between native and denatured lysozyme becomes independent of the temperature over a range of 60 K. The importance of taking into account non-ideality of a mixed solution, when analyzing preferential solvation phenomena was emphasized.	acetonitrile	14-18	lysozyme	Homo sapiens	166-174	
10631479-7	2000	At the higher MeCN content this dependence decreases until, at 0.06 mole fractions of MeCN, the difference in the preferential solvation between native and denatured lysozyme becomes independent of the temperature over a range of 60 K. The importance of taking into account non-ideality of a mixed solution, when analyzing preferential solvation phenomena was emphasized.	acetonitrile	86-90	lysozyme	Homo sapiens	166-174	
28576085-0	2017	Lysozyme in water-acetonitrile mixtures: Preferential solvation at the inner edge of excess hydration.	acetonitrile	18-30	lysozyme	Homo sapiens	0-8	
9567173-0	1998	[Elastic properties of triclinic crystals of lysozyme in anhydric acetonitrile].	acetonitrile	66-78	lysozyme	Homo sapiens	45-53	
9567173-1	1998	Measurements of lysozyme crystal elastic properties in anhydrous acetonitrile were performed in order to investigate the role of water in protein elasticity.	acetonitrile	65-77	lysozyme	Homo sapiens	16-24	
9567173-2	1998	It was shown that triclinic crystals of lysozyme are suitable for such kind of investigation because of being placed in acetonitrile they save crystal lattice parameters.	acetonitrile	120-132	lysozyme	Homo sapiens	40-48	
18618457-5	1994	The solubility of lysozyme, both in an individual solvent (1,5-pentanediol) and in binary solvent mixtures (DMSO/acetonitrile), markedly increased when the pH of the enzyme aqueous solution prior to lyophilization was moved away from the proteins"s isoelectric point.	acetonitrile	113-125	lysozyme	Homo sapiens	18-26	
28576085-2	2017	Organic solvent/water sorption and residual enzyme activity measurements were performed to monitor the preferential solvation/hydration of hen egg-white lysozyme at high and low water content in acetonitrile at 25  C. The obtained results show that the protein destabilization/stabilization depends essentially on the initial hydration level of lysozyme and the water content in acetonitrile.	acetonitrile	195-207	lysozyme	Homo sapiens	153-161	
28576085-4	2017	At high water content, the lysozyme has a higher affinity for water than for acetonitrile.	acetonitrile	77-89	lysozyme	Homo sapiens	27-35	
28576085-6	2017	At the intermediate water content, the dehydrated lysozyme has a higher affinity for acetonitrile than for water.	acetonitrile	85-97	lysozyme	Homo sapiens	50-58	
28576085-13	2017	At low water content, the preferential binding of the acetonitrile molecules to the initially hydrated lysozyme was detected.	acetonitrile	54-66	lysozyme	Homo sapiens	103-111	
27027849-5	2016	When eluted with a suitable pH gradient, salt concentration gradient, and acetonitrile content gradient, the separation behavior of bovine serum albumin and lysozyme could be controlled by altering the conditions of the mobile phase.	acetonitrile	74-86	lysozyme	Homo sapiens	157-165