4.1.1.18	42000	-	2 * 42000, SDS-PAGE	654982	
4.1.1.18	44000	-	2 * 44000, SDS-PAGE	37290	
4.1.1.18	76500	-	2 * 76500, SDS-PAGE	728013	
4.1.1.18	79000	-	7 * 79000, SDS-PAGE	37300	
4.1.1.18	80000	-	10 * 80000, SDS-PAGE	37299	
4.1.1.18	80000	-	? * 80000, SDS-PAGE, under native conditions aggregation of up to 10 subunits	37283	
4.1.1.18	80000	-	x * 80000, equilibrium ultracentrifugation in 6 M guanidine-HCl, SDS-PAGE. Association of the dimeric form to the decamer is concomitant with the increase in ionic strength	37289	
4.1.1.18	80000	-	x * 80000, SDS-PAGE, high-speed sedimentation equilibrium in presence of 6 M guanidine HCl. Subunits associate or dissociate reversibly as a function of pH and ionic strength. The native decameric form is formed by the cyclic association of five dimers. Its overall appearance is that of two stacked pentameric rings. Higher aggregates result from the linear stacking of decamers to form rodlike particles of indefinite length	37293	
4.1.1.18	81000	-	10 * 81000, X-ray crystallography	716768	
4.1.1.18	82000	-	SDS-PAGE	690597	
4.1.1.18	85000	-	x * 85000, SDS-PAGE	727766	
4.1.1.18	88000	-	gel filtration	37290, 654982	
4.1.1.18	95000	-	gel filtration	37297	
4.1.1.18	150000	-	gel filtration	728013	
4.1.1.18	154000	-	dimeric enzyme form, sedimentation data	37289	
4.1.1.18	158000	-	dimeric enzyme, native PAGE	748418	
4.1.1.18	422000	-	pentameric enzyme form, native PAGE	37283	
4.1.1.18	531000	-	gel filtration	37300	
4.1.1.18	545000	-	heptameric enzyme form, gel filtration	37283	
4.1.1.18	730000	-	decameric enzyme form, sedimentation data	37289	
4.1.1.18	761000	-	decameric enzyme form, analytical ultracentrifugation at 6800 rpm	37283	
4.1.1.18	780000	-	decameric enzyme, native PAGE	748418	
4.1.1.18	795700	-	decameric enzyme form, analytical ultracentrifugation at 3600 rpm	37283	
4.1.1.18	800000	-	gel filtration	37299	
4.1.1.18	1000000	-	equilibrium sedimentation	37294, 37295	
4.1.1.18	1174000	-	pentadecameric enzyme form, analytical ultracentrifugation at 2600 rpm	37283