1.2.1.31	dimer	2 * 54000, quantitative sedimentation analysis	
1.2.1.31	monomer	1 * 155000, SDS-PAGE	
1.2.1.31	additional information	ALDH7A1 forms a dimer-of-dimers tetramer both in crystallo and in solution. NAD+-binding promotes assembly of the ALDH7A1 tetramer and enhances ALDH7A1 tetramerization at micromolar enzyme concentrations. The apoenzyme is mainly dimeric. NAD+-bound ALDH7A1 is predominantly tetrameric. The tetramer is the active form of the enzyme. The catalytically active oligomer of ALDH7A1 is assembled on demand in response to cofactor availability. The major peaks correspond to Mr of 110 kDa and 184 kDa, which are both below the theoretical Mr of the tetramer (222 kDa), consistent with an intermediate exchange regime in which free dimer exists in solution simultaneously with a dimer-tetramer equilibrium. The minor species at 2.7S (54 kDa) likely represents a monomer (theoretical Mr of 56 kDa)	
1.2.1.31	tetramer	4 * 54000, quantitative sedimentation analysis