Prinz W A, Beckwith J
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115.
J Bacteriol. 1994 Oct;176(20):6410-3. doi: 10.1128/jb.176.20.6410-6413.1994.
To compare two approaches to analyzing membrane protein topology, a number of alkaline phosphatase fusions to membrane proteins were converted to beta-lactamase fusions. While some alkaline phosphatase fusions near the N terminus of cytoplasmic loops of membrane proteins have anomalously high levels of activity, the equivalent beta-lactamase fusions do not. This disparity may reflect differences in the folding of beta-lactamase and alkaline phosphatase in the cytoplasm.
为了比较两种分析膜蛋白拓扑结构的方法,许多与膜蛋白融合的碱性磷酸酶被转化为β-内酰胺酶融合蛋白。虽然一些位于膜蛋白细胞质环N端附近的碱性磷酸酶融合蛋白具有异常高的活性水平,但相应的β-内酰胺酶融合蛋白却没有。这种差异可能反映了β-内酰胺酶和碱性磷酸酶在细胞质中折叠方式的不同。