Journal
PROTEIN EXPRESSION AND PURIFICATION
Volume 45, Issue 1, Pages 241-248Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2005.08.007
Keywords
Mycobacterium tuberculosis; pyrroline-5-carboxylate reductase; Rv0500; proC; protein expression
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Pyrroline-5-carboxylate reductase (P5CR) plays an important role in the survival of Mycobacterium tuberculosis and is related to virulence of this pathogen. RT-PCR analysis indicated that proC, encoding P5CR, was expressed at the transcriptional level cultured in vitro. The His-rMtP5CR with an N-terminal His-tag (His-rMtP5CR) was firstly purified in Escherichia coli and rMtP5CR was obtained by removal of the N-terminal fusion partner using enterokinase. His-rMtP5CR had considerable beta-pleated sheet analyzed by circular dichroism spectroscopy. The effect of pit, temperature, cations, denaturants, and detergents on the purified enzyme activity and stability was characterized. The N-terminal fusion partner was Found to have very little effect on the biochemical properties of P5CR. (C) 2005 Elsevier Inc. All rights reserved.
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