PURIFICATION AND PARTIAL CHARACTERIZATION OF THE OPACITY-ASSOCIATED PROTEINS OF NEISSERIA-GONORRHOEAE
PURIFICATION AND PARTIAL CHARACTERIZATION OF THE OPACITY-ASSOCIATED PROTEINS OF NEISSERIA-GONORRHOEAE
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DOI：
10.1084/jem.159.2.452
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发表时间：
1984-01-01
影响因子：
15.3
通讯作者：
GOTSCHLICH, EC
中科院分区：
文献类型：
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作者：
BLAKE, MS;GOTSCHLICH, EC
在琼脂上生长的淋球菌经常产生不透明的菌落。这种不透明表型与.gtoreq的存在有关。1 .apprx的外膜蛋白。28000兆瓦。这些蛋白质被包括在一类名为蛋白质II的蛋白质中。本文描述了一种从淋病奈瑟菌中分离纯化不透明蛋白的方法。该方法使用高浓度Ca和pH为4.0的两性离子洗涤剂。在这些条件下，蛋白II很容易从外膜溶解。在两性离子洗涤剂的存在下，通过离子交换和分子筛层析进一步提纯。不透明度相关蛋白是非常碱性的，等电点为9.0-10.0。它们在离子交换色谱上的行为和它们的氨基酸组成进一步证明了它们的基本性质。
Gonococci, grown on agar, frequently gave rise to opaque colonies. This opacity phenotype was associated with the presence of .gtoreq. 1 outer membrane proteins of .apprx. 28,000 MW. These proteins were included within a class of proteins named proteins II. A method is described to isolate and purify the opacity-associated proteins from N. gonorrhoeae. This method used high concentrations of Ca and a zwitterionic detergent at pH 4.0. Under these conditions proteins II were readily solubilized from the outer membrane. Further purification was achieved by ion exchange and molecular sieve chromatography in the presence of the zwitterionic detergent. The opacity-associated proteins were very basic with isoelectric points of 9.0-10.0. Further evidence for their basic nature was their behavior on ion exchange chromatography and their amino acid composition.