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J Antimicrob Chemother. 1998 Jul;42(1):95-8.

Interaction of ceftriaxone with penicillin-binding proteins of Escherichia coli in the presence of human serum albumin.

Author information

1
Istituto di Microbiologia, Università di Verona, Italy.

Abstract

The binding of ceftriaxone, a cephalosporin that exhibits high serum protein binding and prolonged serum half-life, to penicillin-binding proteins (PBPs) of Escherichia coli K12 in the presence of human serum albumin was compared with plasma concentrations of cefotaxime, a cephalosporin with low serum protein binding and a short serum half-life. Ceftriaxone concentrations equivalent to those maintained in plasma for 8 h after an intravenous infusion of 1 g saturated PBPs 2 and 3. Cefotaxime saturated both PBPs at concentrations equivalent to those maintained for 2 h, and PBP 3 only at concentrations maintained for 2-8 h. These results indicate that high serum protein binding does not impair the ability of ceftriaxone to inhibit essential PBPs, and explain the high in-vivo efficacy of the drug.

PMID:
9700535
DOI:
10.1093/jac/42.1.95
[Indexed for MEDLINE]

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