Hommel R, Kleber H P
Bereich Biochemie der Sektion Biowissenschaften der Karl-Marx-Universität Leipzig, DDR.
J Basic Microbiol. 1990;30(4):297-300. doi: 10.1002/jobm.3620300418.
An improved solubilization procedure for the membrane-bound quinoprotein aldehyde dehydrogenase from Acetobacter rancens CCM 1774 was established. After the first solubilization of membrane enzymes by Brij 35 which provided important extraction of membrane proteins other than aldehyde dehydrogenase, the application of Trition X-100 resulted in an almost 20-fold purification of quinoprotein aldehyde dehydrogenase. The optimal solubilization was closely connected with definite detergent/protein ratios.
建立了一种改进的增溶方法，用于从 rancens 醋杆菌 CCM 1774 中提取膜结合的醌蛋白醛脱氢酶。先用 Brij 35 对膜酶进行首次增溶，这能重要地提取除醛脱氢酶之外的膜蛋白，之后使用 Triton X-100 可使醌蛋白醛脱氢酶的纯化倍数几乎达到 20 倍。最佳增溶效果与特定的去污剂/蛋白质比例密切相关。
