雷氏变形杆菌产生的β-内酰胺酶的纯化及生化特性
Purification and biochemical properties of beta-lactamase produced by Proteus rettgeri.
作者信息
Matsuura M, Nakazawa H, Inoue M, Mitsuhashi S
出版信息
Antimicrob Agents Chemother. 1980 Nov;18(5):687-90. doi: 10.1128/AAC.18.5.687.
Abstract
beta-Lactamase produced by Proteus rettgeri was found to be a typical cephalosporin beta-lactamase on the basis of its substrate hydrolysis profile. The enzyme activity was enhanced by prior treatment with an inducer. The enzyme was purified 166-fold by carboxymethyl-Sephadex column chromatography which indicated that its molecular weight was 42,000 +/- 2,000 and its isoelectric point was 8.7. Cefoperazone, cefoxitin, cefusulodin, cefmetazole, cefotaxime, 6059-S, FK749, YM-09330, carbenicillin, and cloxacillin were stable to this enzyme and possessed the function of competitive inhibition, as shown by their affinity for the beta-lactamase. The enzyme activity was inhibited by iodine, p-chloromerburibenzoate, and HG2+ ion. Clavulanic acid and CP-45899 displayed poor inhibitory activity toward this enzyme. The optimal pH was 8.0, and the optimal temperature was 50 degrees C.
摘要
根据雷氏变形杆菌产生的β-内酰胺酶的底物水解谱，发现其为典型的头孢菌素β-内酰胺酶。用诱导剂预处理可增强该酶的活性。通过羧甲基-葡聚糖凝胶柱色谱法将该酶纯化了166倍，结果表明其分子量为42,000±2,000，等电点为8.7。头孢哌酮、头孢西丁、头孢磺啶、头孢美唑、头孢噻肟、6059-S、FK749、YM-09330、羧苄西林和氯唑西林对该酶稳定，并具有竞争性抑制作用，这从它们对β-内酰胺酶的亲和力可以看出。该酶的活性受到碘、对氯汞苯甲酸和汞离子的抑制。克拉维酸和CP-45899对该酶的抑制活性较弱。最适pH为8.0，最适温度为50℃。
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