PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
91367-8	1979	Electrophoresis of S-alpha 2M in the presence of sodium dodecylsulphate gave results consistent with the view that the alpha 2M molecule is a tetramer of identical subunits, assembled as a non-covalent pair of disulphide-linked dimers.	disulphide	210-220	alpha-2-macroglobulin	Homo sapiens	119-127	
91367-15	1979	Exposure of S-alpha 2M to 3 M-urea or pH3 resulted in dissociation to the disulphide-bonded half-molecules; these did not show the proteinase-binding activity characteristic of the intact alpha 2M.	disulphide	74-84	alpha-2-macroglobulin	Homo sapiens	14-22	
91367-19	1979	F-alpha 2M formed by reaction with a proteinase or ammonium salts was not dissociated under the same conditions, although the interchain disulphide bonds were reduced.	disulphide	137-147	alpha-2-macroglobulin	Homo sapiens	2-10