Reference: Berhe A, et al. (1995) Expression and purification of the high-affinity phosphate transporter of Saccharomyces cerevisiae. Eur J Biochem 227(1-2):566-72

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Abstract


The plasma membrane high-affinity phosphate permease of Saccharomyces cerevisiae has been overproduced as a stable membrane-bound chimeric protein in Escherichia coli. Construction of a chimera between the permease and a peptide containing 10 consecutive histidine residues allowed selective binding of the chimera to a chelating column charged with Ni2+, and elution with imidazole in a high state of purity. Approximately 5 mg purified His10-permease was obtained from 3 g (wet mass) cells. The purified phosphate permease chimera catalyzes uncoupler-sensitive phosphate transport after reconstitution into proteoliposomes.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Berhe A, Fristedt U, Persson BL
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