PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2153117-5	1990	Here we have applied ligand and immunoblotting to visualize the Xenopus laevis oocyte receptor for vitellogenin as a protein with an apparent Mr of 115,000 in sodium dodecyl sulfate-polyacrylamide gels under nonreducing conditions.	polyacrylamide	182-196	a1-a	Xenopus laevis	99-111	
849274-17	1977	These precursor data fit in well with structural studies on serum vitellogenin, since it has been shown that the latter protein consists of two identical subunits each with a mobility on sodium dodecyl sulphate/polyacrylamide gels identical with that shown by the microsomal precursor.	polyacrylamide	211-225	a1-a	Xenopus laevis	66-78	
7217071-7	1981	This is further supported by the analysis of newly synthesized and assembled [3H,32P]vitellogenin on sodium dodecyl sulfate-polyacrylamide gels and measurements of protein kinase activity in microsomal subfractions.	polyacrylamide	124-138	a1-a	Xenopus laevis	85-97	
1270438-4	1976	The in vitro product and [14C]vitellogenin co-migrate on electrophoresis in sodium dodecyl sulfate-polyacrylamide gels and they exhibit identical immunoprecipitation curves.	polyacrylamide	99-113	a1-a	Xenopus laevis	30-42	
1117004-10	1975	The major component of vitellogenin labeled wither in vivo or in culture has a molecular weight of approximately 180,000 as shown by sodium dodecyl sulfate polyacrylamide gel electrophoresis.	polyacrylamide	156-170	a1-a	Xenopus laevis	23-35