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- W1418552687 abstract "This chapter discusses the assay method and purification procedure of β-lactamases (actinomycetes species). They are completely inactivated by heating at 60 ° for 5 min. The albus G β-lactamase is sensitive to dilution; activity is remained and assays are performed in the presence of 10% glycerol (w/v; final concentration). The assay method is the microscale adaptation of the technique of Novick and Dubnau. Acetate buffer, color reagent, and finally the same amount of enzyme as used in the test are added, and the optical density at 620 nm is determined. A decrease of the optical density of 0.1 corresponds to about 0.37 nmole of hydrolyzed benzylpenicillin. In isolation of streptomyces β-lactamases, unless otherwise stated, concentration is carried out by ultrafiltration through UMIO membranes with an Amicon apparatus. During fractionation, it is essential to monitor the collected fractions for β-lactamase and DD-carboxypeptidase activity and to keep for further processing those fractions preferentially enriched in β-lactamase. The β-lactamasc and DD-carboxypeptidase from Streptomyces R39 are anionic proteins at pH 8.3. At this pH, the β-lactamase of Streptomyces albus G is anionic whereas its DD-earboxypeptidase is cationic. The procedures described in the chapter give rise to preparations devoid of any detectable DDcarboxypeptidase activity after periods up to 24 hr of incubation with Ac2-L-Lys-D-Ala-D-Ala." @default.
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- W1418552687 date "1975-01-01" @default.
- W1418552687 modified "2023-09-26" @default.
- W1418552687 title "[53f] β-Lactamases (Actinomycetes species)" @default.
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- W1418552687 doi "https://doi.org/10.1016/0076-6879(75)43134-2" @default.
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