Abstract
A beta-lactamase was extracted from an Escherichia coli K-12 strain carrying the R-TEM plasmid and has been purified by affinity chromatography. Antisera to this enzyme were prepared in the rabbit, and the enzyme-antibody neutralization reaction has been evaluated with acidimetric methods (pH stat or pH meter). Under defined experimental conditions, it is now possible to clearly illustrate the enzyme-antibody reaction by means of accurate, rapid, and simple-to-perform methods. These methods are in accord with the specificity of the two reactive partners and allow the detection of the enzyme in a crude bacterial extract which would eventually contain more than one beta-lactamase.
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