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A comparative study on the inhibitory actions of chloramphenicol, thiamphenicol and some fluorinated derivatives.
- M. Cannon, S. Harford, J. Davies
- Biology, ChemistryThe Journal of antimicrobial chemotherapy
- 1 September 1990
Sch 24893, Sch 25298 and Sch 25393 may have important uses in veterinary and clinical medicine and are shown to be like chloramphenicol in inhibiting peptidyl transferase activity specifically on 70 S ribosomes.
Evidence of isosteric and allosteric nucleotide inhibition of citrate synthease from multiple-inhibition studies.
Evidence is presented, from multiple-inhibition studies on various citrate synthases, that ATP acts in all cases as an isosteric inhibitor at the acetyl-CoA site and NADH also acts isosterically with eukaryotic and Gram-positive bacterial citrate syntheases.
Studies on a mutant form of Escherichia coli citrate synthase desensitised to allosteric effectors.
By mutagenesis and suitable selection, this work has succeeded in isolating a mutant of E. coli whose citrate synthase is both 'small' and insensitive to NADH and 2-oxoglutarate.
Characterization of a loss-of-function mutation in the isopenicillin N synthetase gene of Acremonium chrysogenum.
5-epi-Sisomicin and 5-epi-Gentamicin B: substrates for aminoglycoside-modifying enzymes that retain activity against aminoglycoside-resistant bacteria
- A. Vastola, J. Altschaefl, S. Harford
- Biology, ChemistryAntimicrobial Agents and Chemotherapy
- 1 May 1980
Analysis of partially purified aminoglycoside-modifying enzymes from the strains showed that the 5-epi compounds were substrates even for those enzymes found in susceptible strains, confirming and extending the notion that enzymatic modification of aminocusides is not in itself sufficient to confer resistance to the drugs, but also that the modification must be efficient, as reflected in the Km values.
Mutant citrate synthases from Acinetobacter generated by transformation [proceedings].
- P. Weitzman, H. Kinghorn, L. Beecroft, S. Harford
- BiologyBiochemical Society transactions
- 1 April 1978
The production of mutant forms of the enzyme from Acinetobacter lwofi (a Gram-negative aerobe) by transformation is reported, which might contribute to an understanding of the molecular requirements for the production of a tetrameric, rather than a dimeric, enzyme.
Nucleotide sequences of four variants of the K88 gene of porcine enterotoxigenic Escherichia coli
- C. Dykes, I. J. Halliday, M. J. Read, A. Hobden, S. Harford
- BiologyInfection and immunity
- 1 October 1985
Comparison of the amino acid sequences inferred from the gene sequences revealed certain clusters of amino acid substitutions which have been correlated with areas of potential antigenicity in the mature proteins.
Inactivation of the Escherichia coli heat-labile enterotoxin by in vitro mutagenesis of the A-subunit gene.
- S. Harford, C. Dykes, A. Hobden, M. J. Read, I. J. Halliday
- BiologyEuropean journal of biochemistry
- 1 August 1989
In vitro mutagenesis of the LTA gene, encoding the A subunit of the Escherichia coli heat-labile enterotoxin, has been used to obtain A subunits deficient in enzymic activity, and one inactive A-subunit mutant was shown to associate with native B subunits to form a holotoxoid lacking toxin activity.
Resistance to chloramphenicol in Proteus mirabilis by expression of a chromosomal gene for chloramphenicol acetyltransferase
- I. Charles, S. Harford, J. Brookfield, W. V. Shaw
- Biology, ChemistryJournal of bacteriology
- 1 October 1985
The location of the cat gene within the PstI fragment was determined by Southern blotting with a cat consensus oligonucleotide corresponding to the expected amino acid sequence of the active site region of chloramphenicol acetyltransferase, and the direction of transcription was deduced from homology with the type I cat variant.
Regulation of Isopenicillin N Synthetase (IPNS) Gene Expression in Acremonium Chrysogenum
The rapid appearance of IPNS mRNA in mycelial extracts up to day 2 suggests that IPNS is regulated at the transcriptional level and primer extension and SI endonuclease mapping studies indicate the existence of two major and at least two minor transcription initiation start sites.