PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31445214-2	2019	The aim of the study was to analyze partition of model proteins (lysozyme, bovine serum albumin and hemoglobin) depending on the magnetic field action and the factors mentioned above in PEG/MgSO4 ATPS.	atps	196-200	lysozyme	Homo sapiens	65-73	
19617006-4	2009	Partitioning of lysozyme in PEG-citrate ATPS was enthalpically driven, however the PEG-sulfate ATPS was entropically driven.	atps	40-44	lysozyme	Homo sapiens	16-24	
19617006-5	2009	The tested systems can be employed for the separation of these two proteins in egg white, due to the fact that lysozyme migrates toward the polymeric phase and conalbumin to the saline phase in both ATPS.	atps	199-203	lysozyme	Homo sapiens	111-119	
15881359-5	2005	The major protein components in hen egg white, including ovaltransferrin, ovalbumin and lysozyme also show distinct differences of partition coefficients in PEG1000-phosphate ATPs at pH 9.2.	atps	175-179	lysozyme	Homo sapiens	88-96	
15881359-6	2005	Ovalbumin and lysozyme were successfully purified to homogeneity and ovaltransferrin to ca 60% purity from the hen egg white sample with yields over 90% in 15.0% PEG1000-17.0% phosphate ATPs at pH 9.2 with the apparatus rotating at 850 r/min and mobile phase flow rate of 1.0 mL/min.	atps	186-190	lysozyme	Homo sapiens	14-22