PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2447076-10	1988	The major observations are that despite extensive proteolysis, alpha 2M largely retained its native conformation as shown by rate electrophoresis, the absence of binding of monoclonal antibody F2B2, and the incorporation of [14C]methylamine into a 145-kDa fragment of alpha 2M.	Carbon-14	225-228	alpha-2-macroglobulin	Homo sapiens	63-71	
6179545-8	1982	Trypsin treatment of the [14C]methylamine-labeled AMG and alpha 2 M also sequentially generate subunit patterns indistinguishable from those of the unlabeled macroglobulins.	Carbon-14	26-29	alpha-2-macroglobulin	Homo sapiens	58-67	
6157682-11	1980	A large, 56-amino acid residue glycopeptide derived from tryptic cleavage of [14C]methylamine-labeled alpha 2M was isolated.	Carbon-14	78-81	alpha-2-macroglobulin	Homo sapiens	102-110	
92026-3	1979	The reaction is selective and specific in that only 1 or 2 labeled peptides are observed on radioautography of peptide maps derived from [14C]methylamine-treated alpha 2-macroglobulin.	Carbon-14	138-141	alpha-2-macroglobulin	Homo sapiens	162-183	
2422174-6	1986	14C-Labeled alpha 2M-methylamine was used as an internal marker for the position of the thioesters.	Carbon-14	0-3	alpha-2-macroglobulin	Homo sapiens	12-20	
6189480-5	1983	[14C]Methylamine incorporation was 4.1, 3.9, 2.6 and 3.2 mol/mol of proteinase inhibitor for human alpha 2M, rat alpha 1M, rat alpha 2M and mouse alpha 2M, respectively.	Carbon-14	1-4	alpha-2-macroglobulin	Homo sapiens	99-107	
6180729-2	1982	The present results confirm our previous findings that disruption of the internal thioesters, is not in itself sufficient to cause the conformational change of alpha 2M typical of alpha 2-M-proteinase complexes; the electrophoretically slow form of alpha 2M with [14C]methylamine incorporated was isolated.	Carbon-14	264-267	alpha-2-macroglobulin	Homo sapiens	249-257