2.3.3.8	?	-	488221	
2.3.3.8	?	x * 105000, SDS-PAGE	488190	
2.3.3.8	?	x * 110000, SDS-PAGE	488188	
2.3.3.8	?	x * 120000, SDS-PAGE	488221, 488224	
2.3.3.8	?	x * 120608, calculated, identified by mass spectrometry	704077	
2.3.3.8	?	x * 123000, SDS-PAGE	488186	
2.3.3.8	?	x * 125000, SDS-PAGE	488210, 704077	
2.3.3.8	?	x * 43675 + y * 65535, calculated, x * 40000 + x * 65000, SDS-PAGE	658601	
2.3.3.8	?	x * 55000 + x * 70000, may have hexameric structure, SDS-PAGE	-, 488216	
2.3.3.8	?	x * 66000, SDS-PAGE	659954	
2.3.3.8	heterohexamer	3 * 70000 + 3 * 55000	-, 719383	
2.3.3.8	hexamer	6 * 43000, SDS-PAGE	-, 488211	
2.3.3.8	homotetramer	-	718760, 757453, 758520	
2.3.3.8	homotetramer	4 * 110000, SDS-PAGE	718938	
2.3.3.8	homotetramer	4 * 120000, MALDI TOF mass spectrometry	-, 736127	
2.3.3.8	homotetramer	4 * 120100, calculated from amino acid sequence	-, 736127	
2.3.3.8	additional information	N-terminal amino acid sequence	658601	
2.3.3.8	octamer	4 * 45000 + 4 * 65000, SDS-PAGE	488222	
2.3.3.8	tetramer	-	757803	
2.3.3.8	tetramer	4 * 110000, SDS-PAGE	488199	
2.3.3.8	tetramer	4 * 116000, SDS-PAGE	488191	
2.3.3.8	tetramer	4 * 12000, gel filtration in presence of 6 M guanidinium chloride	488200	
2.3.3.8	tetramer	4 * 120000, the two minor proteins 51000 Da and 49000 Da can be the result of proteolytic cleavage of ATP:citrate lyase by an endogenous trypsin-like proteinase	488217	
2.3.3.8	tetramer	4 * 135000, SDS-PAGE	488209	
2.3.3.8	tetramer	ACLY C-terminal citrate synthase homology domain maintains ACLY tetramerization, a conserved and essential quaternary structure. ATP-citrate lyase multimerization is required for coenzyme-A substrate binding and catalysis	757232	
2.3.3.8	tetramer	the tetramer comprises four identical subunits, each resulting from the fusion of N-terminal citryl-CoA synthetase module and the catalytic C-terminal citryl-CoA lyase domain	756333