id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-317070-awip52k7	nan	Molecular characterization of two human autoantigens: unique cDNAs encoding 95- and 160-kD proteins of a putative family in the Golgi complex	1993-07-01		.txt	text/plain	7360	436	55	Changes to the structure and distribution of the Golgi complex antigens were followed by indirect immunoperoxidase staining (47) using the prototype serum SY, rabbit antibodies to the recombinant SY2, SY10, and SYll proteins, and affnity-pufifed antibodies as described above. When antibodies from the prototype serum were affinity purified on nitrocellulose filters containing 5 x 104 phage-expressing SY2 and SYll recombinant proteins, all reproduced the Golgi pattern of immunofluorescence on HEp-2 cells (Fig. 1 b) . The 35S-labeled in vitro translation product of SYll cDNA migrated in SDS-PAGE at 95 kD ( Fig. 8 b, lane I) and was immunoprecipitated by the original human anti-Golgi serum (Fig. 8 b, lane 3) . Evidence that the rabbit antiserum raised by immunization with recombinant SY11 recognized the same protein as the prototype human serum was shown when the rabbit antiserum immunoprecipitated the in vitro translation product in an identical manner to human Golgi sera (Fig. 8 b, compare lanes 3 and 5 with lane 4).	./cache/cord-317070-awip52k7.txt	./txt/cord-317070-awip52k7.txt