Heimann W, Klaiber V
Z Lebensm Unters Forsch. 1977 Dec 9;165(3):144-6. doi: 10.1007/BF01650746.
It was attempted to separate isomerase and lipoperoxidase activity from oat by means of gel and ion exchange chromatography and by isoelectric focusing. The molecular weight of the enzyme fraction tested was found to be of the order of 3 X 10(6) daltons. By ion exchange chromatography and isoelectric focusing the enzyme fraction with lipoperoxidase and isomerase activity could be separated into isoenzymes. These isoenzymes continued to exhibit both enzymatic activities. The lack of success in achieving of separation and the high molecular weight lead to the conclusion of the asistence of a close interrelation between the two enzymes or possibly of a bifunctional enzyme complex.
尝试通过凝胶色谱、离子交换色谱和等电聚焦从燕麦中分离异构酶和脂过氧化酶活性。测试的酶组分的分子量约为3×10⁶道尔顿。通过离子交换色谱和等电聚焦，具有脂过氧化酶和异构酶活性的酶组分可分离成同工酶。这些同工酶继续表现出两种酶活性。分离未成功以及高分子量导致得出这两种酶之间存在密切相互关系或可能存在双功能酶复合物的结论。
