Veser J, Geywitz P, Thomas H
Z Naturforsch C Biosci. 1979 Sep-Oct;34(9-10):709-14. doi: 10.1515/znc-1979-9-1010.
In an effort to investigate catechol methyltransferase activity in sources other than mammalian tissues and cells, a high level of enzyme activity was found in the yeast fungus Candida tropicalis CBS 94. Partial purification of the enzyme (approx. 550 fold with a recovery of 7%) could be achieved by using ion-exchange and gel filtration techniques. The molecular weight was estimated at 32,000 +/- 2,000 by gel filtration on Sephadex G-100. In isoelectric focusing experiments on Sephadex G-75 the enzyme exhibited a pI-value of 5.0 +/- 0.1. In contrast to catechol methyltransferase from various mammalian tissues the enzyme activity was prepared from the pH 5-sediment. The substrate specifity is comparable to other catechol methyltransferases.
为了研究除哺乳动物组织和细胞以外的其他来源中的儿茶酚甲基转移酶活性，在热带假丝酵母CBS 94这种酵母真菌中发现了高水平的酶活性。通过使用离子交换和凝胶过滤技术可以实现该酶的部分纯化（约550倍，回收率为7%）。通过在Sephadex G - 100上进行凝胶过滤，估计分子量为32,000±2,000。在Sephadex G - 75上进行的等电聚焦实验中，该酶的pI值为5.0±0.1。与来自各种哺乳动物组织的儿茶酚甲基转移酶不同，该酶活性是从pH 5的沉淀物中制备的。底物特异性与其他儿茶酚甲基转移酶相当。
