AFFINITY CHROMATOGRAPHIC ISOLATION OF PERIPLASMIC MALTOSE BINDING-PROTEIN OF ESCHERICHIA-COLI
AFFINITY CHROMATOGRAPHIC ISOLATION OF PERIPLASMIC MALTOSE BINDING-PROTEIN OF ESCHERICHIA-COLI
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DOI：
10.1016/0014-5793(78)80940-5
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发表时间：
1978-01-01
期刊：
影响因子：
3.5
通讯作者：
KLOTZ, U
中科院分区：
文献类型：
--
作者：
FERENCI, T;KLOTZ, U
The periplasmic, osmotic-shock releasable maltose binding protein is one of at least four gene products that make up the maltose transport system of Escherichia coli [I]. A further component is an outer membrane protein known as the phage X receptor [2] which is obligatory for the permeation of longer maltodextrins into the cell [3]. The gene products of the malF and malK genes are also necessary for maltose transport [4] and at least the ma/F product is likely to be an inner membrane protein [5]. In addition to its transport function, the periplasmic binding protein also acts as chemoreceptor in taxis towards maltose [6].In order to study the proteins involved in the process of transport (and chemotaxis), it was of interest to prepare an affinity chromatographic material satisfying the substrate requirements of the transport system (and chemoreceptor). It has been demonstrated that the maltose transport system is also responsible for the entry of maltodextrins into the cell and that the binding protein recognizes not only maltose but also maltodextrins up to at least maltoheptaose [3]. This communication demonstrates that amylose crosslinked by epichlorohydrin also satisfies the substrate specificity of the maltose binding protein and hence provides a simple affinity chromatographic substrate for studies of maltose recognition in transport and chemotaxis. It also permits a rapid, one step purification of the maltose binding protein from osmotic-shock fluids.
