Matheis G, Belitz H D
Z Lebensm Unters Forsch. 1977 Apr 28;163(4):279-82. doi: 10.1007/BF02425362.
Gel chromatography on Sephadex G-200 was used to separate a soluble phenoloxidase from potatoes (var. Maritta) into at least six active fractions with dopa (dihydroxyphenylalanine) as substrate. Only high-molecular-weight-enzyme forms exhibited monophenoloxidase activity. Re-chromatography of the highest-molecular-weight form gave the same molecular weight distribution as with the crude enzyme. The molecular weights indicate association phenomena of subunits with a molecular weight of about 36000 daltons. According to polyacrylamide-gel electrophoresis, several monomeric forms with differnt isoelectric points seem to be present. This suggests that the large number of multiple forms of the enzyme arises from various combinations of identical and/or different subunits. SDS polyacrylamide gel electrophoresis failed to show the monomeric forms; the dimer and higher oligomers were obtained.
采用葡聚糖凝胶G - 200凝胶色谱法，以多巴（二羟基苯丙氨酸）为底物，将马铃薯（品种为玛丽塔）中的一种可溶性酚氧化酶分离成至少六个活性组分。只有高分子量的酶形式表现出单酚氧化酶活性。对最高分子量形式进行再色谱分析，得到的分子量分布与粗酶相同。分子量表明存在分子量约为36000道尔顿的亚基缔合现象。根据聚丙烯酰胺凝胶电泳，似乎存在几种具有不同等电点的单体形式。这表明该酶的多种形式是由相同和/或不同亚基的各种组合产生的。SDS聚丙烯酰胺凝胶电泳未能显示出单体形式；得到了二聚体和更高的寡聚体。
