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Redesigned purification yields a fully functional...
Journal article

Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli.

Abstract

Proline utilization by Escherichia coli and Salmonella typhimurium requires expression of genes putP (encoding a proline transporter) and putA. Genetic data indicate that the PutA protein is both put repressor and a respiratory chain-linked dehydrogenase. We report a redesigned purification procedure as well as the physical characteristics and biological activities of the PutA protein purified from E. coli. The purified protein was homogeneous …

Authors

Brown ED; Wood JM

Journal

Journal of Biological Chemistry, Vol. 267, No. 18, pp. 13086–13092

Publisher

Elsevier

Publication Date

June 1992

DOI

10.1016/s0021-9258(18)42384-8

ISSN

0021-9258