Results 271 to 280 of about 1,753,858 (323)
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Presence of Beta-Lactamase–Producing Bacteria and Beta-Lactamase Activity in Abscesses

American Journal of Clinical Pathology, 1986
The presence of beta-lactamase-producing bacteria (BLPB) in abscesses was investigated in 109 abscesses. Single isolates were recovered in 23 (21%) instances and were predominantly Staphylococcus aureus. The other abscesses yielded growth of two or more aerobic and/or anaerobic organisms.
openaire   +2 more sources

Contribution of beta-lactamases to bacterial resistance and mechanisms to inhibit beta-lactamases

The American Journal of Medicine, 1985
Resistance of bacteria to beta-lactam antibiotics has become a serious problem in the past several decades. Virtually all Staphylococcus aureus, and many Hemophilus influenzae, Branhamella catarrhalis, Neisseria gonorrhoeae, Enterobacteriaceae, and Bacteroides species possess beta-lactamases that hydrolyze penicillins and cephalosporins.
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Beta-lactamase inhibitor combinations

Medical Clinics of North America, 1995
The beta-lactamase inhibitor combinations present a novel approach to the problem of beta-lactamase-induced resistance to antibiotics. These agents are derived from the generally safe beta-lactam class of antibiotics. They are all principally excreted through the kidneys and require dosage adjustment in the face of significant renal insufficiency. They
J W, Sensakovic, L G, Smith
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Beta-lactamases and beta-lactamase inhibitors.

International journal of antimicrobial agents, 1999
Penicillin, the first of the beta-lactam antibiotics, was introduced into medical practice in the 1940s. Since then, a large number of different beta-lactams, including penicillins, cephalosporins, monobactams, and carbapenems, have been developed, all of which are structurally related through the presence of a core beta-lactam ring. Resistance to beta-
openaire   +1 more source

Newer Penicillins and Beta-Lactamase Inhibitors

Infectious Disease Clinics of North America, 1989
Penicillins continue to be essential antibiotics for the treatment and prophylaxis of many infectious diseases. Recent advances have resulted in compounds with favorable new antimicrobial and pharmacologic properties. This article reviews the spectrum of activity, toxicity, pharmacokinetics, and clinical uses of the extended spectrum penicillins and ...
L M, Bush, J, Calmon, C C, Johnson
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Metallo Beta Lactamase Enzymes

Indian Journal of Microbiology
Multidrug resistance has become more common in Gram-negative bacteria, making them one of the emerging public health problems with extremely detrimental effects on the world economy. These drugs are broad-spectrum-lactam antibiotics used as a last-resort treatment against multidrug-resistant microorganisms (MDROs).
Sawsan Mohammed Kareem   +2 more
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Zinc Beta Lactamase Superfamily

2013
The metallo-beta-lactamase superfamily was first defined in 1997 on the basis of a sequence alignment. The members of this superfamily are characterized by the presence of a common alpha-beta-beta-alpha fold and share five conserved motifs: Asp84, His116-Xaa-His118-Xaa-Asp120-His121, His196, Asp221 and His263, which are (with the exception of Asp84 ...
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Induction of beta-lactamases.

The Journal of antimicrobial chemotherapy, 1989
Inducible beta-lactamases can significantly affect the activities of both beta-lactamase-stable and beta-lactamase-sensitive antibiotics. beta-Lactam antibiotics vary in their ability to induce beta-lactamases. Strong inducers can antagonize the antimicrobial activity of other beta-lactams.
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The structure of beta-lactamases.

Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 1980
R. Ambler
semanticscholar   +1 more source

Cefotetan and beta-lactamases. I. An analysis of the affinity of cefotetan for beta-lactamases.

The Journal of antimicrobial chemotherapy, 1983
Cefotetan is a new cephamycin whose interaction with a group of eight beta-lactamases isolated from various Gram-negative bacteria has been studied. Using computerized micro-acidimetry, cefotetan was found to be resistant to the hydrolytic action of various enzymes, including those which actively hydrolyse cefotaxime.
R, Labia   +3 more
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