PubMed · 7105993
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L A Morris, S C Groft. 1982. Patient package inserts: a research perspective.. https://pubmed.ncbi.nlm.nih.gov/7105993/
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Anionic phospholipids have been shown to interact with both membrane-associated proteins and integral membrane proteins. The objective of this work was to determine whether bacteriolysis induced by treatment with ampicillin was influenced by the levels of anionic membrane phospholipids in Escherichia coli strain HDL11. The pgsA gene, encoding phosphatidylglycerophosphate synthase, in HDL11 is under the control of lacOP, and the levels of anionic membrane phospholipids are consequently dependent on IPTG. The results indicate that limiting the amounts of phosphatidylglycerol and cardiolipin did not affect the lysis process in both growing and nongrowing bacteria.
Diagnostic imaging and treatment of unilateral destructive temporomandibular joint disease in two horses is described and discussed. Computed tomography appeared to be the best imaging technique for these lesions. The disease can be followed by functional recovery after the infection has resolved.
A rapid and sensitive HPLC method was developed for the determination of ampicillin residues in muscle tissues of beef, pork, chicken and catfish. Muscle tissues were blended with a food processor into paste. A 5-g aliquot of the blended tissues was homogenized with 14 ml of 0.01 M phosphate buffer (pH 4.5) using a tissue homogenizer. Proteins were precipitated with the addition of 1 ml trichloroacetic acid (75%, w/v) followed by centrifugation. After filtration, 1 ml of the supernatant was reacted with formaldehyde under acidic and heating conditions. The ampicillin fluorescent derivative was then analyzed by reverse phase HPLC with fluorescence detection. Recoveries of spiked ampicillin at 5, 10 and 20 ng/g were >85%, with coefficients of variation <5%. The limit of detection and limit of quantitation for ampicillin in the tissues were 0.6 ng/g and 1.5 ng/g, respectively. The method is also applicable to the analysis of ampicillin residue in dry milk powder.