PURIFICATION OF PROTEIN A, AN OUTER MEMBRANE COMPONENT MISSING IN ESCHERICHIA-COLI K-12 OMPA MUTANTS
PURIFICATION OF PROTEIN A, AN OUTER MEMBRANE COMPONENT MISSING IN ESCHERICHIA-COLI K-12 OMPA MUTANTS
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DOI：
10.1016/0005-2795(77)90274-4
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发表时间：
1977-01-01
期刊：
影响因子：
--
通讯作者：
FOULDS, J
中科院分区：
文献类型：
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作者：
CHAI, TJ;FOULDS, J
从大肠杆菌ompA （tolG）菌株制备的外膜材料不含ompA+菌株中发现的主要外膜蛋白之一。该蛋白在含有十二烷基硫酸钠的聚丙烯酰胺凝胶中通过制备电泳，从ompA+菌株制备的洗涤剂溶解细胞包膜材料中获得了高产量。纯化后的蛋白在3个电泳体系中均质，含有2 mol的还原糖/mol的肽，n端氨基酸为丙氨酸。氨基酸组成与从不完全溶解的细胞包膜材料中纯化的外膜蛋白II*或B*几乎相同。外膜蛋白II*或B*难以溶解的部分与较易溶解的部分相同。
Outer membrane materials prepared from an E. coli ompA (tolG) strain do not contain one of the major outer membrane proteins found in ompA+ strains. This protein was purified in high yield from detergent-solubilized cell envelope material prepared from an ompA+ strain by preparative electrophoresis in polyacrylamide gels containing sodium dodecyl sulfate. The purified protein is homogeneous in 3 electrophoretic systems, contains 2 mol of reducing sugar/mol of peptide and has alanine as the N-terminal amino acid. Amino acid composition is nearly identical to outer membrane protein II* or B* purified by others from incompletely solubilized cell envelope material. The fraction of outer membrane protein II* or B* that is difficult to solubilize is identical with the more readily solubilized fraction.