1.10.3.3	?	x * 61268, deduced from amino acid sequence	439903	
1.10.3.3	?	x * 62258, deduced from amino acid sequence	439903	
1.10.3.3	?	x * 62800, calculated from amino acid sequence	742708	
1.10.3.3	?	x * 64000, SDS-PAGE	439903	
1.10.3.3	dimer	-	439890, 672768	
1.10.3.3	dimer	1 * 74000 + 1 * 62000, SDS-PAGE	439930	
1.10.3.3	dimer	2 * 30000, enzyme exists as monomer, dimer and tetramer, SDS-PAGE	439924	
1.10.3.3	dimer	2 * 65000, treatment with 2-mercaptoethanol results in 2 new bands, an A chain of 38000 Da and an B chain of 28000 Da, SDS-PAGE	439925	
1.10.3.3	dimer	2 * 70000, 70000 Da subunit consists of 2 polypeptide chains of 30000 and 40000 Da respectively	439890	
1.10.3.3	dimer	2 * 72000, basic enzyme, SDS-PAGE	439938	
1.10.3.3	dimer	unfolding studies, pressure-induced and denaturing agents-induced dissociation and unfolding, and the role of dimerization in the folding strategy of a large protein, crystal structure analysis, physico-chemical properties of a molten dimer enzyme, three distinct domains per subunit, sharing a common beta-barrel topology, overview	673569	
1.10.3.3	dodecamer	12 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE	439924	
1.10.3.3	heterodimer	1 * 72000 + 1 * 75000	764566	
1.10.3.3	homodimer	ascorbate oxidase is a large, multidomain, dimeric protein	724962	
1.10.3.3	monomer	1 * 30000, enzyme also exists as dimer and tetramer, SDS-PAGE	439924	
1.10.3.3	monomer	1 * 35000, enzyme also exists as tetramer, octamer, dodecamer and polymer, SDS-PAGE	439924	
1.10.3.3	monomer	1 * 80000	-, 439929	
1.10.3.3	additional information	each subunit is devided into 3 domains	439902	
1.10.3.3	additional information	quarternary structure	439925	
1.10.3.3	additional information	structure analysis: the monomers keep their secondary structure, whereas subtle conformational changes in the tertiary structure become apparent, salt bridges and electrostatic interactions occurring at the dimeric interface play a crucial role in the stabilization of the monomer's tertiary structure., folding/unfolding pathway, overview. Each subunit is formed by three distinct domains and contains four copper ions, three of which are located at the interface between domains, forming a so-called trinuclear centre	724962	
1.10.3.3	octamer	8 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE	439924	
1.10.3.3	polymer	x * 35000, between 670000 Da and 2000000 Da, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE	439924	
1.10.3.3	tetramer	4 * 30000, enzyme exists as monomer, dimer and tetramer, SDS-PAGE	439924	
1.10.3.3	tetramer	4 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE	439924	
1.10.3.3	tetramer	4 * 70000, tetramer with D2 symmetry, crystal structure and SDS-PAGE, present as dimer in solution. Each subunit is built up by three domains arranged sequentially on the polypeptide chain and tightly associated in space. The folding of all three domains is of a similar beta-barrel type, analysis of intra- and intertetramer hydrogen bond and van der Waals interactions, domains structures, detailed overview	717986