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[地衣芽孢杆菌青霉素酶。β-内酰胺抗生素酶促水解产物电离常数的测定]

[Penicillinase from B. licheniformis. Determination of the ionization constants of the enzymatic hydrolysis products of beta-lactam antibiotics].

作者信息

Satarova D E, Nys P S, Korchagin V B, Savitskaia E M

出版信息

Antibiotiki. 1984 Jan;29(1):14-9.

PMID:6607709
Abstract

The level of transformation of beta-lactam antibiotics hydrolysed by penicillinase from B. licheniformis on determination with the method of pH-metric titration with sodium hydrate solutions depended on the electrochemical nature of the products formed. The data on the study of the pH dependence of the penicillinase-catalysed hydrolysis of beta-lactam antibiotics were used for estimation of the ionization constants of the products of the enzymatic hydrolysis of the beta-lactam ring in the molecules of azlocillin, carfecillin, benzylpenicillin, cephalothin and 7-PADCA. Methods for quantitative determination of the compounds were developed. The methods are based on penicillinase-catalysed enzymatic hydrolysis and pH-metric titration of the products with sodium hydrate solutions at pH 7.0 with regard to their dissociation levels.

摘要

用氢氧化钠溶液进行pH滴定法测定时,地衣芽孢杆菌青霉素酶水解β-内酰胺抗生素的转化程度取决于所形成产物的电化学性质。β-内酰胺抗生素青霉素酶催化水解的pH依赖性研究数据用于估算阿洛西林、羧苄青霉素、苄青霉素、头孢噻吩和7-氨基去乙酰氧基头孢烷酸分子中β-内酰胺环酶促水解产物的电离常数。开发了这些化合物的定量测定方法。这些方法基于青霉素酶催化的酶促水解以及在pH 7.0下根据产物解离程度用氢氧化钠溶液进行pH滴定。

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