Sawai T, Takahashi I, Yamagishi S
Antimicrob Agents Chemother. 1978 Jun;13(6):910-3. doi: 10.1128/AAC.13.6.910.
The rapid fixed-time assay for penicillinase was modified for measuring beta-lactamase activity with twelve substrates, i.e., benzylpenicillin, ampicillin, cloxacillin, methicillin, carbenicillin, cefazolin, cephalothin, cephaloglycin, cephalexin, cephalosporin C, 7-aminocephalosporanic acid, and cefoxitin. The method depends upon the reduction of iodine by the hydrolyzed substrate. Determined experimentally, 1 mol of hydrolyzed penicillins consumed 3.4 to 4.0 mol of iodine (I(2)). Iodine consumption of hydrolyzed cephalosporins varied widely from 1.7 for cephalothin to 3.7 for cefazolin. The method is useful for routine assay of beta-lactamase activity with various substrates.
青霉素酶快速定时测定法经改进后用于测定十二种底物的β-内酰胺酶活性,这些底物包括苄青霉素、氨苄青霉素、氯唑西林、甲氧西林、羧苄青霉素、头孢唑林、头孢噻吩、头孢甘氨酸、头孢氨苄、头孢菌素C、7-氨基头孢烷酸和头孢西丁。该方法基于水解底物对碘的还原作用。通过实验测定,1摩尔水解青霉素消耗3.4至4.0摩尔碘(I₂)。水解头孢菌素的碘消耗量差异很大,从头孢噻吩的1.7到头孢唑林的3.7不等。该方法可用于常规测定各种底物的β-内酰胺酶活性。