2.3.1.135	?	x * 20900	720353	
2.3.1.135	?	x * 25000, about	719417	
2.3.1.135	?	x * 25000, recombinant enzyme	658662	
2.3.1.135	?	x * 25000, SDS-PAGE	658661	
2.3.1.135	?	x * 26000, calculated from sequence, x * 29000, SDS-PAGE	758200	
2.3.1.135	dimer	2 * 25000, full-length wild-type enzyme, SDS-PAGE, 2 * 20000, recombinant truncated enzyme, SDS-PAGE	658001	
2.3.1.135	homodimer	2 × 25300, SDS-PAGE in presence of 2-mercaptoethanol	638623	
2.3.1.135	homodimer	SDS-PAGE in absence of 2-mercaptoethanol	638623	
2.3.1.135	monomer	-	638619, 638620, 638623	
2.3.1.135	monomer	1 * 25000, full-length wild-type enzyme, SDS-PAGE, 1 * 20000, recombinant truncated enzyme, SDS-PAGE	658001	
2.3.1.135	monomer	1 × 25000, fully active catalytically	638617	
2.3.1.135	monomer	1 × 25300, SDS-PAGE in presence of 2-mercaptoethanol, fully active catalytically	638617	
2.3.1.135	monomer	1 × 25800, fully active catalytically	638619	
2.3.1.135	additional information	epitope mapping, the enzyme contains a C-terminal transmembrane domain	674832	
2.3.1.135	additional information	LRAT monomer interact in membranes and form functional homodimers, the dimer formation is mediated by disulfide bond formation and protein-protein interactions	638623	
2.3.1.135	additional information	the enzyme exists as a mixture of monomer and dimer, determined by sedimentation equilibrium analysis and mass spectrometry, higher aggregation, up to pentamers, occurs in absence of denaturing agents	658001