Koller E, Koller F, Hoffmann-Ostenhof O
Mol Cell Biochem. 1976 Jan 31;10(1):33-9. doi: 10.1007/BF01731679.
Enzyme preparations from oat seedlings showing the activity of myo-inositol oxygenase (E.C.1.13.99.1) have been described previously. In contrast to myo-inositol oxygenase preparations from other sources, e.g. rat kidney or yeast, the oat enzyme seemed to exhibit a somewhat less stringent activity, acting on other inositols and inositol methyl ethers as well as on myo-inositol. By purification of the enzyme present in the extract from oat seedlings with the help of an affinity gel specific for enzymes acting on myo-inositol a homogeneous enzyme preparation was obtained, which shows the same strict specificity as the myo-inositol oxygenase from other sources. It has a molecular weight of 62,000 and tends to aggregate to oligomers (up to tetramers) under physiological pH-values; in more alkaline media dissociation to monomers is observed. The action on the other inositols and inositol methyl ethers is apparently due to one or more other enzymes, which are also adsorbed on the affinity gel, but can be separated from the myo-inositol oxygenase by elution with increasing concentrations of myo-inositol.
此前已有关于燕麦幼苗中显示肌醇加氧酶（E.C.1.13.99.1）活性的酶制剂的描述。与来自其他来源（如大鼠肾脏或酵母）的肌醇加氧酶制剂不同，燕麦酶似乎表现出不太严格的活性，它不仅作用于肌醇，还作用于其他肌醇和肌醇甲醚。借助对作用于肌醇的酶具有特异性的亲和凝胶，对燕麦幼苗提取物中的酶进行纯化，得到了一种均一的酶制剂，它显示出与来自其他来源的肌醇加氧酶相同的严格特异性。它的分子量为62,000，在生理pH值下倾向于聚合成寡聚体（高达四聚体）；在更碱性的介质中会观察到解离成单体。对其他肌醇和肌醇甲醚的作用显然是由于一种或多种其他酶，这些酶也吸附在亲和凝胶上，但可以通过用浓度逐渐增加的肌醇洗脱而与肌醇加氧酶分离。
