PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3158653-1	1985	The tryptophan intrinsic fluorescence of the (Ca2+ + Mg2+)-ATPase from sarcoplasmic reticulum was quenched by acrylamide at different temperatures.	Acrylamide	110-120	dynein axonemal heavy chain 8	Homo sapiens	59-65	
133717-5	1976	The ATPase has an apparent molecular weight of approximately 100 000 as determined by electrophoresis in acrylamide gels containing dodecyl sulphate.	Acrylamide	105-115	dynein axonemal heavy chain 8	Homo sapiens	4-10	
6105878-8	1980	By means of histochemical activity staining in acrylamide gels it was shown that the purified ATPase preparation could be inhibited by Cd2+ and Zn2+ salts, p-chloromercuribenzoate and N-ethylmaleimide, known inhibitors of membrane endocytosis.	Acrylamide	47-57	dynein axonemal heavy chain 8	Homo sapiens	94-100	
8388334-1	1993	Circular dichroism (CD) and acrylamide quenching studies of Na+,K(+)-ATPase from human placenta showed that its incorporation into phosphatidylcholine vesicles increased the enzymic activity by 55%.	Acrylamide	28-38	dynein axonemal heavy chain 8	Homo sapiens	69-75	
2150904-3	1990	Moreover, quenching of the ATPase intrinsic fluorescence by acrylamide indicated that, depending on the enzyme conformational status, the accessibility of its tryptophan residues is influenced by direct interaction with CaM at micromolar Ca2+ concentration.	Acrylamide	60-70	dynein axonemal heavy chain 8	Homo sapiens	27-33