news
GOVERNMENT AND SOCIETY Enzyme-based defense against GHB cloned the DNA that encodes for the enzyme. They then inserted the cloned DNA into E. coli, which makes large amounts of the enzyme in a form that can be easily isolated. “One liter of culture makes enough enzyme for 10,000 tests,” Parsons says.
“A perpetrator has to put only 2 g of GHB in a 4-oz drink to reduce a 125-lb person to putty in their hands.” — Stanley Parsons GHB DH catalyzes the reaction between GHB and the cofactor NAD+, producing NADH. Although monitoring the formation of NADH can be useful for qualitative purposes, the conversion is not quantitative and cannot be seen with the naked eye. To make the assay quantitative, the DH reaction has to be coupled to another reaction that is thermodynamically favorable and produces a visible color change. To accomplish this, Parsons and colleagues used a second enzyme, diaphorase, which reoxidizes NADH back to NAD+ by reducing a colorless dye precursor. Upon reduction of the dye precursor, a colored product forms in seconds if GHB is present. The amount of GHB in urine that the body produces naturally is typically
