6.3.4.16	32000	-	2 * 32000, SDS-PAGE	1473	
6.3.4.16	34360	-	-	651213	
6.3.4.16	41403	-	2 * 41403, calculated from amino acid sequence	728172	
6.3.4.16	44000	-	2 * 44000, SDS-PAGE	728172	
6.3.4.16	46600	-	1 * 46600, SDS-PAGE	722163	
6.3.4.16	50700	-	gel filtration	722163	
6.3.4.16	55000	-	1 * 130000 + 1 * 55000, SDS-PAGE	1474	
6.3.4.16	78000	80000	native PAGE, gel filtration	1473	
6.3.4.16	91000	-	gel filtration	728172	
6.3.4.16	120000	-	2 * 120000, SDS-PAGE	1456	
6.3.4.16	130000	-	1 * 130000 + 1 * 55000, SDS-PAGE	1474	
6.3.4.16	140000	-	gel filtration	674389	
6.3.4.16	158000	-	1 * 158000, sedimentation equilibrium in 6 M guanidine hydrochloride containing DTT, predominantly exists in the monomeric form	1467	
6.3.4.16	160000	-	1 * 160000, SDS-PAGE in presence of a reducing agent	1463	
6.3.4.16	160000	-	1 * 160000, sedimentation velocity measurement in presence of acetylglutamate alone, enzyme exists in a rapid, reversible monomer-dimer equilibrium. In presence of all substrates the enzyme exists as a monomer. The activator N-acetyl-L-glutamate displaces the equilibrium towards monomer formation	1461	
6.3.4.16	160000	-	x * 160000, SDS-PAGE	1465	
6.3.4.16	160000	251000	sedimentation velocity measurement, gel filtration, MW depends on protein concentration and composition of solvent	1456	
6.3.4.16	163700	-	x * 163700, calculated from amino acid sequence	728044	
6.3.4.16	165000	-	-	652202	
6.3.4.16	165000	-	1 * 165000, SDS-PAGE	1464	
6.3.4.16	165000	-	2 * 165000, SDS-PAGE of carboxymethylated enzyme	1470	
6.3.4.16	165000	178000	gel filtration, density gradient centrifugation	1463	
6.3.4.16	166000	-	mass spectrometry	693935	
6.3.4.16	188000	-	gel filtration	1474	
6.3.4.16	190000	-	gel filtration	1464	
6.3.4.16	192000	-	recombinant enzyme, gel filtration	727610	
6.3.4.16	202000	-	native enzyme, gel filtration	727610	
6.3.4.16	222000	-	glycerol or sucrose density gradient centrifugation	1456	
6.3.4.16	250000	-	gel filtration	1470