Proteomics
Random mutagenesis affects B. subtilis glutamate dehydrogenase thermostability
Published in Gene Therapy Weekly, January 5th, 2006
"Bs-GluDH was cloned, and expressed at considerable magnitude in Escherichia coli," wrote M.I.H. Khan and colleagues, Shimane University.
"The recombinant Bs-GluDH was purified to homogeneity and has been determined to have a hexameric structure (Mr 270 kDa) with strict specificity for 2-oxoglutarate and L-glutamate, requiring NADH and NAD+ as cofactors respectively."
The researchers wrote, "The enzyme showed low thermostability...
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Source: Gene Therapy Weekly (2006-01-05)
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