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Biomedical subjects

T J Munton

Publications and source records attributed to T J Munton.

9 recordsLinked to original sources
PubMed1985

The stability of sodium nitroprusside infusion during administration by motorized syringe-pump.

This study examined the stability of concentrated sodium nitroprusside infusions during administration by a motorized syringe-pump system. Sodium nitroprusside and the free-cyanide degradation product were determined in infusion samples collected over periods of up to 24 h. Measures which were taken to protect the delivery system from light, ensured satisfactory stability of the infusion for at least 12 h from the time of preparation.

Cyanides↗
PubMed1984

Particle size measurement in intravenous fluids.

The level of particulate contamination in a range of large volume injections has been measured using electrical resistance (Coulter) and light blockage (HIAC) techniques. Particle counts showed large variations between the two techniques and although a correlation could be shown for ionic solutions no such correlation could be found for sugar containing solutions. Shape factors alone cannot explain these discrepancies but other differences fundamental to the physics of the two measuring techniques play an important part. We conclude that results obtained using one technique cannot be correlated, theoretically or actually, with those obtained from the other technique.

Electric Conductivity↗
PubMed1973

Effect of glutaraldehyde on cell viability, triphenyltetrazolium reduction, oxygen uptake, and beta-galactosidase activity in Escherichia coli.

Acid (pH 5) and alkaline (pH 8.5) glutaraldehyde solutions were compared for their effects on cell viability, oxygen uptake, and beta-galactosidase activities in Escherichia coli. The action of glutaraldehyde at pH 7 on dehydrogenase activity was also studied. Dehydrogenase activity was inhibited at aldehyde concentrations which had little effect on cell viability. In contrast, oxygen uptake and beta-galactosidase activity took place in cells killed by acid or alkaline glutaraldehyde. The effect of glutaraldehyde on dehydrogenase activity and beta-galactosidase activity of disrupted suspensions was also investigated. The dialdehyde was considerably less inhibitory to these enzyme systems than to those of whole cells, and it is thus feasible that the results with whole cells are a consequence of its interaction with, and strengthening of, the outer cell surface, thereby preventing ready access of substrate to enzyme.

Aldehydes↗