PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9331967-1	1997	The catalytic activity of superoxide dismutase (SOD) and its conjugates with catalase and polymer peroxidase (p-peroxidase) obtained during covalent binding of enzymes with aldehyde dextrans was indirectly characterized by inhibition of adrenaline autoxidation in 0.1 M bicarbonate buffer, pH 10.2, and in microemulsion of 0.1 M aerosol OT (AOT) and Triton X-45 in octane containing 15% aqueous phase.	Dioctyl Sulfosuccinic Acid	341-344	superoxide dismutase 1	Homo sapiens	26-46	
9331967-1	1997	The catalytic activity of superoxide dismutase (SOD) and its conjugates with catalase and polymer peroxidase (p-peroxidase) obtained during covalent binding of enzymes with aldehyde dextrans was indirectly characterized by inhibition of adrenaline autoxidation in 0.1 M bicarbonate buffer, pH 10.2, and in microemulsion of 0.1 M aerosol OT (AOT) and Triton X-45 in octane containing 15% aqueous phase.	Dioctyl Sulfosuccinic Acid	341-344	superoxide dismutase 1	Homo sapiens	48-51