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本文报告以紫外分光光度法测定两种β-内酰胺酶抑制剂——克拉维酸和青霉烷砜对β-内酰胺酶水解头孢噻啶、头孢盂多和头孢哌酮的抑制率。实验结果表明,以头孢噻啶为底物时,0.1mM的克拉维酸和青霉烷砜对受试的 7种质粒介导的β-内酰胺酶均具有强大抑制作用,但在1、0.5μg/ml时,则前者的抑酶活性远较后者为强。以头孢盂多为底物时,除OXA-2外,克拉维酸对其余6种质粒酶的抑制作用较青霉烷砜强。以头孢哌酮为底物时,青霉烷砜对TEM-1、TEM-2、PSE-2、PSE-4和SHV-1的抑酶活性较弱。值得注意的是,青霉烷砜对OXA-2水解 3种底物的抑酶作用均较克拉维酸为强。克拉维酸和青霉烷砜对两种染色体酶D31和K-1均几无抑酶活性。
This article reports the inhibition of β-lactamase hydrolysis of ceftazidime, cefdinid and cefoperazone by UV spectrophotometry of two β-lactamase inhibitors, clavulanic acid and penicillin sulfone. The experimental results show that, with cefotaxime as substrate, clavulanic acid and penicillin 0.1mM 0.1mg of the seven plasmid-mediated beta-lactamase were strong inhibitory effect, but at 1,0.5 μg / ml, then the former inhibition of the enzyme activity is far stronger than the latter. To cephaladone as substrate, in addition to OXA-2, clavulanic acid on the remaining six kinds of plasmid enzyme inhibition than penicillin sulfone. When cefoperazone was used as substrate, penicillin sulfone had weaker inhibitory activity against TEM-1, TEM-2, PSE-2, PSE-4 and SHV-1. It is noteworthy that penicillin sulfone on OXA-2 hydrolysis of the three substrate inhibition of the enzyme than clavulanic acid is stronger. Clavulanic acid and penicillin sulfone pairs of the two chromosomal enzymes D31 and K-1 almost no inhibition of enzyme activity.