PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
151100-4	1978	Gel chromatography in presence or absence of Tween 80 gives rise to formation of oligomers of various size and smaller amounts of monomeric ATPase.	Polysorbates	45-53	dynein axonemal heavy chain 8	Homo sapiens	140-146	
2148657-2	1990	NaF (mM) completely inhibits the Ca-ATP-ase activity in presence of 0.02% tween-20.	Polysorbates	74-82	dynein axonemal heavy chain 8	Homo sapiens	36-43	
152120-5	1978	The fragmented ATPase retained the same specific activity and stability as the intact ATPase under a variety of conditions when solubilized in Tween 80 or dodecyl octaoxyethylene glycol monoether.	Polysorbates	143-151	dynein axonemal heavy chain 8	Homo sapiens	15-21	
152120-5	1978	The fragmented ATPase retained the same specific activity and stability as the intact ATPase under a variety of conditions when solubilized in Tween 80 or dodecyl octaoxyethylene glycol monoether.	Polysorbates	143-151	dynein axonemal heavy chain 8	Homo sapiens	86-92	
151100-11	1978	The binding of Tween 80 by soluble ATPase above the critical micellar concentration is 0.23 to 0.29 g/g of protein.	Polysorbates	15-23	dynein axonemal heavy chain 8	Homo sapiens	35-41	
151100-12	1978	The inactive monomer of ATPase binds phospholipid and Tween 80 to about the same extent, but has a slightly different circular dichroism spectrum, than oligomeric ATPase.	Polysorbates	54-62	dynein axonemal heavy chain 8	Homo sapiens	24-30	
132186-4	1976	Preliminary molecular weight measurements indicate that the Ca2+ -ATPase exists as an oligomer in the native membrane: fully active enzyme in Tween 80 has a minimal protein molecular weight of about 400 000, corresponding to a trimer or tetramer of the ATPase polypeptide chain, and even the inactive enzyme in deoxycholate contains a substantial fraction of dimeric protein.	Polysorbates	142-150	dynein axonemal heavy chain 8	Homo sapiens	66-72	
132186-4	1976	Preliminary molecular weight measurements indicate that the Ca2+ -ATPase exists as an oligomer in the native membrane: fully active enzyme in Tween 80 has a minimal protein molecular weight of about 400 000, corresponding to a trimer or tetramer of the ATPase polypeptide chain, and even the inactive enzyme in deoxycholate contains a substantial fraction of dimeric protein.	Polysorbates	142-150	dynein axonemal heavy chain 8	Homo sapiens	253-259