id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-004672-0lf5j8lo	Anderson, Kevin	Structural and physiological properties of mengovirus: Avirulent, hemagglutination-defective mutants express altered alpha (1 D) proteins and are adsorption-defective	1987		.txt	text/plain	5703	298	59	In this communication, the structurM proteins of the wfld-ty]pe and mutant, viruses were compared by SDS-PAGE, peptide mapping, and twodimensional gel electrophoresis to determine which of the mutant structural proteins differed from that of wild-type and the extent of homology among analogous proteins. To determine whether the arrangement of the structural proteins on the surface of mutants 205 and 280 was similar to that of wild-type, purified virions were labeled with r25I and analyzed by SDS-PAGE (Fig. 2) . Eight virus-specified intracellular proteins were resolved in wild-type and mutant strain-infected cells: A (1-2 A), B (1), C (3), D (3 CD), 1 ABC, D 2 (1 CD), alpha (1 D), and gamma (1 C). To further examine these viruses for structural differences, surface labeling of intact wild-type and mutant virus particles was done to compare the arrangement of the structural proteins which form the xdral capsids.	./cache/cord-004672-0lf5j8lo.txt	./txt/cord-004672-0lf5j8lo.txt