| Literature DB >> 3529391 |
Abstract
Fusions of the secreted protein alkaline phosphatase to an integral cytoplasmic membrane protein of Escherichia coli showed different activities depending on where in the membrane protein the alkaline phosphatase was fused. Fusions to positions in or near the periplasmic domain led to high alkaline phosphatase activity, whereas those to positions in the cytoplasmic domain gave low activity. Analysis of alkaline phosphatase fusions to membrane proteins of unknown structure may thus be generally useful in determining their membrane topologies.Entities:
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Year: 1986 PMID: 3529391 DOI: 10.1126/science.3529391
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728