In situ detection of beta-lactamase activity in sodium dodecyl sulfate-polyacrylamide gels.
After beta-lactamase had been denatured by boiling in the presence of sodium dodecyl sulfate (SDS) and then electrophoresed in SDS-polyacrylamide gels, activity could be restored and could be detected in situ as specific molecular species. Renaturation was simple and facilitated by the presence of a carrier protein. The assay was sensitive, detecting 0.8 ng beta-lactamase activity in the gel.
D001407:Bacillus / Q000201:enzymology; D001426:Bacterial Proteins; D002352:Carrier Proteins; D055598:Chemical Phenomena; D002621:Chemistry; D003101:Collodion; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology; D011489:Protein Denaturation; D001618:beta-Lactamases / Q000032:analysis*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D003101:Collodion; D001618:beta-Lactamases