chloramine-t and sodium-thiosulfate

Treatment of skin with chlorine generates 'chlorine covers' which, in a previous study, exerted significant sustained bactericidal effects against transient skin flora on the upper arm and forearm. In this investigation, this effect was studied on both the transient and resident flora of the hands using test models for the evaluation of hand disinfectants as agreed upon in Austria and Germany. Chlorine covers were generated by bathing hands in a solution of 2% sodium tosylchloramide for 1 min. Subsequently, this cover was destroyed on one, randomly selected, hand by bathing it in a solution of 0.5% sodium thiosulphate for 15 s. The amount of chlorine on the fingertips of chlorinated hands was 2.2 +/- 0.4 micrograms/cm2; that on subsequently dechlorinated hands was 0.2 +/- 0.1 microgram/cm2. In experiments with artificially contaminated hands (Escherichia coli), the kinetics of bacterial die-off were the same on both hands. Also, in experiments with resident flora, the kinetics of bacterial die-off did not suggest bacterial reductions that increase with the duration of contact with the chlorine cover. It was concluded that with the test models used, a significant sustained antimicrobial effect of the chlorine cover could not be demonstrated on hands.

Topics: Animals; Anti-Infective Agents, Local; Bacteria; Chloramines; Disinfectants; Escherichia coli; Hand; Hand Disinfection; Humans; Thiosulfates; Tosyl Compounds

A protocol is described for coupling of carrier-free iodine to protein sulfhydryl groups via fluorescein maleimide. 125I is first coupled to fluorescein maleimide in the presence of chloramine T. Iodination is stopped with sodium thiosulfate, and the iodine-substituted fluorescein maleimide is reacted with free cysteines of the protein. Excess label is then removed by gel-permeation chromatography. The procedure avoids exposition of the protein to oxidative conditions and does not require purification of the labeled carrier reagent. Suitability of the method for a given protein can be evaluated spectrophotometrically without employing radioactivity. It can be applied under denaturing conditions and may be particularly useful with mutant proteins carrying engineered single cysteine residues at sites that are not functionally critical.

Topics: Bacterial Proteins; Chloramines; Chromatography, Gel; Complement Hemolytic Activity Assay; Cysteine; Erythrocytes; Fluoresceins; Iodine Radioisotopes; Polymers; Protein Binding; Proteins; Sensitivity and Specificity; Spectrophotometry; Streptolysins; Thiosulfates; Tosyl Compounds