The Activity of Haemophilus Influenzae ß-Lactamase
H. influenzae ß-lactamase was found to closely resemble the E. coli TEM, ß-lactamase in its substrate profile and rate of hydrolysis of benzyl penicillin, ampicillin and cephaloridine. The permeability barrier to ampicillin and benzyl penicillin observed in the E. coli strain was not detected in the Haemophilus influenzae strain as judged by the activity of whole cell suspensions. It is concluded therefore that this difference is responsible for the smaller amounts of ampicillin required to inhibit ß-lactamase producing strains of H.influenzae compared to strains of E. coli producing ß-lactamase.
KeywordsBenzyl Penicillin Haemophilus Influenzae Permeability Barrier Minimum Inhibitory Concentra Substrate Profile
Unable to display preview. Download preview PDF.