PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2887428-2	1987	To have a better insight into the role of the guanidinium group in D-amino-acid oxidase we have carried out inactivation studies using phenylglyoxal as an arginine-directed reagent.	Guanidine	46-57	D-amino acid oxidase	Homo sapiens	67-87	
6133558-1	1983	The renaturation of free and Sepharose-immobilized D-amino-acid oxidase (D-amino-acid:oxygen oxidoreductase (deaminating), EC 1.4.3.3), after its denaturation with 6 M guanidine hydrochloride, was investigated.	Guanidine	168-191	D-amino acid oxidase	Homo sapiens	51-71	
6131067-0	1982	Thermodynamic characterization of hog kidney D-amino acid oxidase apoenzyme in concentrated guanidine hydrochloride solution.	Guanidine	92-115	D-amino acid oxidase	Homo sapiens	45-65	
6131067-2	1982	This paper describes the physical characterization of the monomeric unit of hog kidney D-amino acid oxidase apoenzyme in 6 M guanidine hydrochloride (GuHCl) solution by means of differential refractometry, densimetry, light scattering, equilibrium sedimentation, and high-speed gel filtration chromatography.	Guanidine	125-148	D-amino acid oxidase	Homo sapiens	87-107	
6131067-2	1982	This paper describes the physical characterization of the monomeric unit of hog kidney D-amino acid oxidase apoenzyme in 6 M guanidine hydrochloride (GuHCl) solution by means of differential refractometry, densimetry, light scattering, equilibrium sedimentation, and high-speed gel filtration chromatography.	Guanidine	150-155	D-amino acid oxidase	Homo sapiens	87-107