[Evaluation of SMBG values using various instruments and clinical significance of forearm SMBG measurement].

Whole blood or plasma glucose values were compared between those measured using various instruments for SMBG and automated analyses in samples (antecubital vein) from 20 approximately 70 years old obtained at cookie tests. A good correlation between values in whole blood SMBG and plasma automated analyses values greater than r = 0.94 was observed for instruments A, C, F, and H, and the per cent difference from the automated values was less than 5% for A, B, E and H. Per cent difference of SMBG values by I was -16% in whole blood and -9% in plasma, suggesting the possibility of measuring real values in whole blood. With plasma, a good correlation greater than r = 0.95 was noted for A, C, F and K, and the per cent difference less than 10% was noted for C, E, F and I. A relatively good correlation (r: 0.63 approximately 0.90) between forearm SMBG value and plasma automated values was noted with the % difference of the mean less than 11%. During cookie test, there is no significant difference between forearm SMBG values and antecubital plasma automated values. Values at finger tips are significantly greater by 5 approximately 20% over automated plasma values. In conclusion, whole blood values by most of the SMBG instruments are well correlated with plasma automated values, although some disagreement was noted. Values at forearm are not different from plasma val ues of antecubital vein, while at finger tip SMBG values showed higher levels. The measurement at forearm is therefore recommended, and in addition the pain is less.

Structure-activity relationship in O-glucuronidation of indolocarbazole analogs.

The glucuronidation of 6-N-formylamino-12,13-dihydro-1,11-dihydroxy-13-(beta-D-glucopyranosyl)5H-indolo[2,3-a]pyrrolo[3,4-c]carbazole-5,7(6H)-dione (compound 1), a potent inhibitor of DNA topoisomerase I, and its related indolocarbazole compounds was studied using human liver microsomes. Compound 1 and its structurally related compounds with the NHCHO moiety at the N-6 position were glucuronidated even if the positions of the phenolic hydroxy moiety were different in these molecules. Compounds that have the NHCH(CH(2)OH)(2) moiety at the N-6 position, however, were not glucuronidated. The three-dimensional structure of these substrates was determined by the semiempirical molecular-orbitals calculation method. Computer-modeling studies, however, revealed that the O-glucuronidation of indolocarbazole analogs depended on the molecular size of the substrates. Compounds larger than 14.5 A in diameter perpendicular to the phenolic hydroxy moiety were not glucuronidated. The chemical reactivity of the hydroxy moiety, evaluated by the atom electron density and the electrostatic potential charges, was very similar in these substrates. These results suggest that a molecular length less than 14.5 A may be required for a substrate to interact with the active site of UDP-glucuronosyltransferase (UGT). To further characterize the glucuronidation of indolocarbazole analogs, compound 1 was used as a representative compound to assess expressed human UGTs. The glucuronidation of compound 1 was catalyzed by recombinant UGT1A9 and UGT1A10 among UGT isoforms tested.