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抗硝酸不动杆菌(同义词:醋酸钙不动杆菌)中的β-内酰胺酶与β-内酰胺类抗生素耐药性

beta-Lactamase and beta-lactam antibiotics resistance in acinetobacter anitratum (syn: A. calcoaceticus).

作者信息

Morohoshi T, Saito T

出版信息

J Antibiot (Tokyo). 1977 Nov;30(11):969-73. doi: 10.7164/antibiotics.30.969.

Abstract

The cephalosporin beta-lactamase (cephalosporinase) produced by Acinetobacter was studied. The enzyme was partially purified by means of column chromatography and its properties were investigated. The enzyme was induced by benzylpenicillin, 6-aminopenicillanic acid and cephaloridine. Its molecular weight is 30,000 its optimal temperature 40C, and its optimal pH 7.25 similar to 7.50. Substrate specificity studies using various cephalosporins and penicillins, showed that the enzyme functioned as a cephalosporinase rather than penicillinase.

摘要

对不动杆菌产生的头孢菌素β-内酰胺酶(头孢菌素酶)进行了研究。通过柱色谱法对该酶进行了部分纯化,并对其性质进行了研究。该酶由苄青霉素、6-氨基青霉烷酸和头孢菌素诱导产生。其分子量为30000,最适温度为40℃,最适pH值为7.25至7.50。使用各种头孢菌素和青霉素进行的底物特异性研究表明,该酶作为头孢菌素酶而非青霉素酶发挥作用。

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