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[酵母细胞中的蛋白质晶体和微管束。VI. 关于分离晶体乙醇脱氢酶活性的光学显微镜、电子显微镜及生化研究]

[Protein crystals and tubuli bundles in yeast cells. VI. Light-and electron microscopy studies as well as biochemical studies on alcohol dehydrogenase activity of isolated crystals].

作者信息

Künkel W

出版信息

Z Allg Mikrobiol. 1977;17(2):109-15. doi: 10.1002/jobm.3630170204.

DOI:10.1002/jobm.3630170204
PMID:868081
Abstract

Isolated crystals from Saccharomyces carlsbergensis, stabilized by Cd2+ or Zn2+, retain their enzymatic activity as shown by topochemical reactions. During these reactions the crystals disintegrate characteristically. Stages of this disintegration and deposition of reaction products have been demonstrated by light and electron microscopy. Ground plasmatic and mitochondrial alcoholdhydrogenase has been solubilized by means of 0.01 M EDTA from Zn2+ stabilized crystals separated by gel electrophoresis and proved to be active.

摘要

通过镉离子或锌离子稳定的卡尔斯伯酵母分离晶体，经拓扑化学反应表明仍保留其酶活性。在这些反应过程中，晶体以特有的方式分解。这种分解阶段及反应产物的沉积已通过光学显微镜和电子显微镜得以证实。通过0.01M乙二胺四乙酸（EDTA）可将经凝胶电泳分离的锌离子稳定晶体中的胞质和线粒体乙醇脱氢酶溶解，且证实其具有活性。

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