McCarthy S A, Johnson R M, Kakimoto D
Department of Botany and Microbiology, Arizona State University, Tempe.
J Appl Bacteriol. 1994 Oct;77(4):426-32. doi: 10.1111/j.1365-2672.1994.tb03445.x.
An antibiotic produced by Alteromonas luteoviolacea strain 9K-V10 was recovered after cold acetone precipitation of culture supernatant fluids or lysates that had been frozen and thawed. The precipitate obtained from cell-free lysates was fractioned by DEAE ion-exchange chromatography. Further purification by gel-filtration chromatography yielded a single peak of antibiotic activity that corresponded to a protein peak with a molecular mass of approximately 100 kDa. After non-denaturing polyacrylamide gel electrophoresis, antibiotic activity co-migrated with a protein band. The isoelectric point of the antibiotic was estimated to be 7.7. Treatment of the concentrated active fraction with proteinase K or heating at 70 degrees C for 10 min resulted in total loss of antibiotic activity. These results show that the antibiotic produced by Alt. luteoviolacea 9K-V10 is of a proteinaceous nature.
在对经冷冻和解冻的培养上清液或裂解物进行冷丙酮沉淀后,从黄色交替单胞菌菌株9K-V10中获得了一种抗生素。通过DEAE离子交换色谱法对无细胞裂解物得到的沉淀物进行分级分离。通过凝胶过滤色谱法进一步纯化后,得到了一个抗生素活性单峰,该单峰对应于一个分子量约为100 kDa的蛋白质峰。在非变性聚丙烯酰胺凝胶电泳后,抗生素活性与一条蛋白带共迁移。该抗生素的等电点估计为7.7。用蛋白酶K处理浓缩的活性级分或在70℃加热10分钟导致抗生素活性完全丧失。这些结果表明,黄色交替单胞菌9K-V10产生的抗生素具有蛋白质性质。