PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25046001-1	2014	Several key properties of catalase such as thermal stability, resistance to protease degradation, and resistance to ascorbate inhibition were improved, while retaining its structure and activity, by conjugation to poly(acrylic acid) (PAA, Mw 8000) via carbodiimide chemistry where the amine groups on the protein are appended to the carboxyl groups of the polymer.	Carbodiimides	252-264	catalase	Homo sapiens	26-34	
21232642-0	2011	Catalase-coupled gold nanoparticles: comparison between the carbodiimide and biotin-streptavidin methods.	Carbodiimides	60-72	catalase	Homo sapiens	0-8	
21232642-6	2011	In the second protocol the formation of an amide bond between carboxylic acid-coated gold nanoparticles and free surface amines of catalase using carbodiimide chemistry was performed.	Carbodiimides	146-158	catalase	Homo sapiens	131-139	
21232642-9	2011	Although the carbodiimide chemistry-based bioconjugation approach exhibited a decrease in catalase activity, the carbodiimide chemistry-based bioconjugation approach resulted in more active catalase per gold nanoparticle compared with that of mercapto-undecanoic acid-stabilized biotinylated gold nanoparticles.	Carbodiimides	113-125	catalase	Homo sapiens	190-198	
21586817-4	2011	CAT enzyme was linked covalently to the surface of iron oxide using carbodiimide in phosphate buffer (pH 7.4) at 4  C. The enzyme-iron oxide link was confirmed by FT-IR spectroscopy.	Carbodiimides	68-80	catalase	Homo sapiens	0-3