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Blood samples Blood samples were collected in Vacutainer Tubes without additives; after separation, the sera were stored at 20 C until analysis. Results assay validation The method used routinely in our laboratory for the diagnosis of abuse of SU drugs was based on liquid-liquid extraction with organic solvents toluene ; , followed by HPLC analysis, as described previously by several authors 1317 ; . To introduce the CE method as a confirmatory method for SU identification in the cases of factitious hypoglycemia, we tried to optimize the preanalytical phase by replacing the classical liquid-liquid extraction with a solid-phase extraction 22 ; . The best results were obtained with a novel sorbent, based on the "universal" OASIS HLB copolymer, designed to separate, in a single chromatographic run, a wide range of compounds with a greater capacity than the classical C18-bonded phase. The recoveries obtained for the different SU drugs in a control serum at 0.5, 2.0, and 10 mg L are shown in Table 1. Because of the improved performance, all analyses reported below by HPLC or CE ; refer to the solid-phase extraction procedure. A typical profile obtained by our reversed-phase HPLC method for screening of SU drugs is shown in Fig. 1. The and evista, because effexor fibromyalgia.
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Discussion Residues 119 and 121 were mutated to study the effect of hydrogen bonding between GA and substrate on substrate specificity. The latter was evaluated not only from kinetic parameters Table II ; but also from formation of iG2 and glucose using highly concentrated glucose and DE 10 maltodextrin, respectively, as substrates Table III ; . The kinetic parameters of Ser119Glu GA showed that this mutation only slightly altered the active site. Catalytic efficiency on short-length substrates, however, was affected more than on long-length substrates. This was possibly due to increased electrostatic interactions from the introduced negative charge near subsite 4 affecting hydrolysis of short-length substrates. Although mutation Ser119Gly was expected to remove the hydrogen bond between residue 119 and the fourth substrate residue to destabilize conformer B, observed changes in G ; did not confirm this. Fersht 1985 ; reported that in certain cases, such as a deletion of an enzyme side-chain allowing the access of water into the enzymesubstrate complex, loss of a hydrogen bond may cause no loss of binding energy. In fact, removal of the Ser119 side-chain by the Ser119Gly mutation potentially allows a water molecule to enter the space between residue 119 and the substrate. The Ser119Gly mutation increased kcat values for G4G7 hydrolysis whereas it decreased them for iG2, G2 and G3 hydrolysis compared with wild-type GA. KM values decreased only for iG2 and G2 hydrolysis. These lower kcat and KM values indicate that the Ser119Gly mutation affected subsites 1 and 2. Since this mutation altered the flexibility of a peptide bond near Trp120, it may affect the side-chain position of Trp120. Trp120 is an important residue, as shown by the effects caused by mutating it Sierks et al., 1989 ; and by three-dimensional structures of GA complexed with pseudotetrasaccharides Stoffer et al., 1995; Aleshin et al., 1996 ; . Atom NE1 of Trp120 hydrogen bonds to atom OE2 of Glu179, the catalytic acid and atoms CE3, CZ3 and CD2 of Trp120 make non-bonded contacts with atom O5 of the third sugar residue of pseudotetrasaccharide inhibitors Figure 1 ; . Sierks et al. 1989 ; reported that mutation of Trp120 to His, Leu, Phe and Tyr decreased kcat and KM 131 and gemfibrozil.

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