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FEBS Lett. 1994 Jun 20;347(1):37-41.

Purification of two active fusion proteins of the Na(+)-dependent citrate carrier of Klebsiella pneumoniae.

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Mikrobiologisches Institut der Eidgenössischen Technischen Hochschule, ETH-Zentrum, Zürich, Switzerland.


The sodium-ion-dependent citrate carrier of Klebsiella pneumoniae (CitS) was purified by means of bioengineerical methods. By fusing the biotin acceptor domain of the alpha-subunit of the oxaloacetate decarboxylase of K. pneumoniae to the C-terminus of CitS, purification of the carrier was achieved by use of a monomeric avidin-Sepharose column. Additionally, we were able to purify a CitS-protein with an N-terminal histidine-tag by immobilized metal chelate affinity chromatography (with Ni2(+)-nitrilotriacetic acid-(NTA-) resin). Both purified fusion proteins showed citrate transport activity after reconstitution into liposomes by the freeze/thaw/sonication procedure.

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