PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7986345-2	1994	Secondary structural changes of the cleaved alpha-lactalbumin, in which the two separated polypeptides were joined by disulfide bridges, were examined in solutions of sodium dodecyl sulfate (SDS), urea, and guanidine hydrochloride.	Urea	197-201	lactalbumin alpha	Homo sapiens	44-61	
7986345-8	1994	On the other hand, the helical structures of the cleaved alpha-lactalbumin began to be disrupted at low concentrations of guanidine hydrochloride and urea compared with that of the intact protein.	Urea	150-154	lactalbumin alpha	Homo sapiens	57-74