Bocillin : Determination of IC 50 s of the penicillin-sensitive and - Subcellular fractions containing bacterial membranes were prepared from 100 ml cultures of .
Incubation of increasing concentrations of bocillin™ fl . Subcellular fractions containing bacterial membranes were prepared from 100 ml cultures of . Cells were grown to late exponential phase and exposed to penicillin g (100 μg/ml). Bocillin™ fl penicillin binding to recombinant pbp 2 at 30°c reached equilibrium. Preparation of samples, pbp labeling of cell lysates with bocillin™ fl and separation of proteins by sodium dodecyl sulfate polyacrylamide .
Preparation of samples, pbp labeling of cell lysates with bocillin™ fl and separation of proteins by sodium dodecyl sulfate polyacrylamide .
Cells were grown to late exponential phase and exposed to penicillin g (100 μg/ml). Preparation of samples, pbp labeling of cell lysates with bocillin™ fl and separation of proteins by sodium dodecyl sulfate polyacrylamide . Bocillin™ fl penicillin binding to recombinant pbp 2 at 30°c reached equilibrium. Subcellular fractions containing bacterial membranes were prepared from 100 ml cultures of . Incubation of increasing concentrations of bocillin™ fl .
Preparation of samples, pbp labeling of cell lysates with bocillin™ fl and separation of proteins by sodium dodecyl sulfate polyacrylamide . Incubation of increasing concentrations of bocillin™ fl . Bocillin™ fl penicillin binding to recombinant pbp 2 at 30°c reached equilibrium. Cells were grown to late exponential phase and exposed to penicillin g (100 μg/ml). Subcellular fractions containing bacterial membranes were prepared from 100 ml cultures of .
Incubation of increasing concentrations of bocillin™ fl .
Bocillin™ fl penicillin binding to recombinant pbp 2 at 30°c reached equilibrium. Preparation of samples, pbp labeling of cell lysates with bocillin™ fl and separation of proteins by sodium dodecyl sulfate polyacrylamide . Incubation of increasing concentrations of bocillin™ fl . Cells were grown to late exponential phase and exposed to penicillin g (100 μg/ml). Subcellular fractions containing bacterial membranes were prepared from 100 ml cultures of .
Incubation of increasing concentrations of bocillin™ fl . Preparation of samples, pbp labeling of cell lysates with bocillin™ fl and separation of proteins by sodium dodecyl sulfate polyacrylamide . Subcellular fractions containing bacterial membranes were prepared from 100 ml cultures of . Bocillin™ fl penicillin binding to recombinant pbp 2 at 30°c reached equilibrium. Cells were grown to late exponential phase and exposed to penicillin g (100 μg/ml).
Preparation of samples, pbp labeling of cell lysates with bocillin™ fl and separation of proteins by sodium dodecyl sulfate polyacrylamide .
Subcellular fractions containing bacterial membranes were prepared from 100 ml cultures of . Cells were grown to late exponential phase and exposed to penicillin g (100 μg/ml). Incubation of increasing concentrations of bocillin™ fl . Preparation of samples, pbp labeling of cell lysates with bocillin™ fl and separation of proteins by sodium dodecyl sulfate polyacrylamide . Bocillin™ fl penicillin binding to recombinant pbp 2 at 30°c reached equilibrium.
Bocillin : Determination of IC 50 s of the penicillin-sensitive and - Subcellular fractions containing bacterial membranes were prepared from 100 ml cultures of .. Subcellular fractions containing bacterial membranes were prepared from 100 ml cultures of . Preparation of samples, pbp labeling of cell lysates with bocillin™ fl and separation of proteins by sodium dodecyl sulfate polyacrylamide . Incubation of increasing concentrations of bocillin™ fl . Cells were grown to late exponential phase and exposed to penicillin g (100 μg/ml). Bocillin™ fl penicillin binding to recombinant pbp 2 at 30°c reached equilibrium.
Incubation of increasing concentrations of bocillin™ fl bocil. Bocillin™ fl penicillin binding to recombinant pbp 2 at 30°c reached equilibrium.
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