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Purification and Characterization of Human Brain Serine Racemase Expressed in Moderately Halophilic Bacteria

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We have successfully expressed an active human brain serine racemase (hSR) with His-tag using moderate halophile. The purified His-hSR showed high elimination and racemization activities on L-serine: the elimination activity was 2.6-fold higher than racemization activity. Both enzyme activities showed an optimum reaction pH at around 9.0 and were stimulated 5- to 7-fold by such divalent cations as Mg++, Mn++ and Ca++.

Keywords: His-tag; Human serine racemase; groE; halophile; porin

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986609787316261

Publication date: February 1, 2009

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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