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ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type.
Proc Natl Acad Sci U S A. 1981 Aug;78(8):4897-901
PMID: 6795623
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6-beta-bromo- and 6-beta-iodo penicillanic acid, two novel beta-lactamase inhibitors.
J Antimicrob Chemother. 1981 May;7(5):531-6
PMID: 6267005
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The exocellular beta-lactamase of Streptomyces albus G. Purification, properties and comparison with the exocellular DD-carboxypeptidase.
Biochem J. 1981 Jan 1;193(1):75-82
PMID: 6975618
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Purification and properties of the exocellular beta-lactamase of Actinomadura strain R39.
Biochim Biophys Acta. 1982 Jan 4;700(1):24-32
PMID: 6976797
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Interaction of clavulanate with the beta-lactamases of Streptomyces albus G and Actinomadura R39.
Biochem J. 1982 Dec 1;207(3):429-36
PMID: 6984651
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Interaction of beta-iodopenicillanate with the beta-lactamases of Streptomyces albus G and Actinomadura R39.
Biochem J. 1982 Dec 1;207(3):437-44
PMID: 6299270
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Comparison of the overlapping frd and ampC operons of Escherichia coli with the corresponding DNA sequences in other gram-negative bacteria.
J Bacteriol. 1983 Sep;155(3):1297-305
PMID: 6350266
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The reversible deactivation of beta-lactamase from Staphylococcus aureus by quinacillin and cephaloridine and its modification by antibodies.
Biochim Biophys Acta. 1984 Mar 29;785(3):104-10
PMID: 6200139
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Kinetics of inactivation of beta-lactamase I by 6 beta-bromopenicillanic acid.
Biochem J. 1980 Jun 1;187(3):797-802
PMID: 6331385
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Purification of beta-lactamases by affinity chromatography on phenylboronic acid-agarose.
Biochem J. 1984 Jul 15;221(2):505-12
PMID: 6332621
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The active site of the P99 beta-lactamase from Enterobacter cloacae.
Biochem J. 1984 Oct 1;223(1):271-4
PMID: 6333871
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Kinetics of suicide substrates. Practical procedures for determining parameters.
Biochem J. 1985 May 1;227(3):843-9
PMID: 4004802
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The beta-lactamase of Enterobacter cloacae P99. Chemical properties, N-terminal sequence and interaction with 6 beta-halogenopenicillanates.
Biochem J. 1985 May 15;228(1):241-8
PMID: 2988516
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The production and molecular properties of the zinc beta-lactamase of Pseudomonas maltophilia IID 1275.
Biochem J. 1985 Aug 1;229(3):791-7
PMID: 3931629
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Sequence of the Citrobacter freundii OS60 chromosomal ampC beta-lactamase gene.
Eur J Biochem. 1986 May 2;156(3):441-5
PMID: 3486121
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Properties of a class C beta-lactamase from Serratia marcescens.
Biochem J. 1986 Nov 1;239(3):581-6
PMID: 3548700
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The beta-lactamase of Streptomyces cacaoi: interaction with cefoxitin and beta-iodopenicillanate.
J Enzyme Inhib. 1985;1(1):25-34
PMID: 2854843
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The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.
J Biol Chem. 1969 Aug 25;244(16):4406-12
PMID: 5806584
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Resistance of Escherichia coli to penicillins. VI. Purification and characterization of the chromosomally mediated penicillinase present in ampA-containing strains.
J Bacteriol. 1970 Jan;101(1):218-31
PMID: 4983650
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Beta-lactamase (Bacillus licheniformis).
Methods Enzymol. 1975;43:653-64
PMID: 1134375
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Beta-lactamase (Enterobacter species).
Methods Enzymol. 1975;43:678-87
PMID: 1169676
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Comparison of beta-lactamase II from Bacillus cereus 569/H/9 with a beta-lactamase from Bacillus cereus 5/B/6.
Biochem J. 1975 Feb;145(2):409-11
PMID: 808215
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The mechanism of folding of globular proteins. Suitability of a penicillinase from Staphylococcus Aureus as a model for refolding studies.
Biochem J. 1976 May 1;155(2):325-30
PMID: 938483
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6-beta-bromopenicillanic acid, a potent beta-lactamase inhibitor.
Proc Natl Acad Sci U S A. 1978 Sep;75(9):4145-9
PMID: 212736
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Inactivation of Bacillus cereus beta-lactamase I by 6 beta-bromopencillanic acid: mechanism.
Biochemistry. 1980 Aug 19;19(17):3996-4003
PMID: 6773559
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On the chemistry of beta-lactamase inhibition by 6 beta-bromopenicillanic acid.
J Chem Soc Perkin 1. 1980;10:2322-9
PMID: 6253512
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The structure of beta-lactamases.
Philos Trans R Soc Lond B Biol Sci. 1980 May 16;289(1036):321-31
PMID: 6109327
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beta-lactamase from Streptomyces cacaoi. Purification and properties.
J Biol Chem. 1981 Mar 25;256(6):2649-55
PMID: 6970744
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6 beta-Iodopenicillanic acid (UI-38,006), a beta-lactamase inhibitor that extends the antibacterial spectrum of beta-lactam compounds: initial bacteriological characterization.
Antimicrob Agents Chemother. 1981 Sep;20(3):327-31
PMID: 6272628