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Biomedical subjects

J W Soper

Publications and source records attributed to J W Soper.

At least 19 recordsLinked to original sources

Prevalence of chlorpheniramine in aviation accident pilot fatalities, 1991-1996.

BACKGROUND: Chlorpheniramine is known to cause drowsiness, and this side effect has a potential to impair performance and could be a factor in accidents. METHODS: Therefore, to establish the prevalence of this drug in pilot fatalities of aviation accidents, a postmortem toxicology database--maintained at the Civil Aeromedical Institute--was examined for the presence of chlorpheniramine in the fatalities, occurred during 1991-1996. RESULTS: There were 47 (2.2%) accidents involving chlorpheniramine. Of these, 16 had only chlorpheniramine at 109 ng.ml-1 (n = 4) in blood and 1412 ng.g-1 (n = 12) in liver. Other drugs were also present in the remaining 31 cases, wherein chlorpheniramine concentrations were 93 ng.ml-1 (n = 18) in blood and 747 ng.g-1 (n = 12) in liver. Ninety-five percent of all quantitated blood values were at or above the therapeutic level (10 ng.ml-1), giving a 100 ng.ml-1 (n = 21) mean blood value. The drug's mean liver concentration from all cases was 1080 ng.g-1 (n = 24). The average blood value was approximately 10 times higher than the therapeutic value. CONCLUSIONS: The presence of other drugs did not appear to significantly alter the blood chlorpheniramine level, but no such correlation could be established with the hepatic value. The approximate 10-fold increase in the liver concentration was consistent with the general trend of drug distribution in the hepatic compartment. However, the contribution of postmortem redistribution of the drug to alter its concentration cannot be entirely ruled out. This study suggests that chlorpheniramine was present in some aviation fatalities at levels higher than therapeutic levels.

Accidents, Aviation↗

Autobiographical pictorial study of a cataract in progress.

The practitioner is all too familiar with the visual complaints of a patient prior to cataract surgery. Unfortunately, these complaints are heard but may not be seriously evaluated by the surgeon as they relate to the patient's daily functional problems. Too frequently Snellen acuity is used as a measure, which can be extremely misleading. This paper will present a number of the patient's complaints and illustrate them as they are seen by the patient to give the surgeon a greater appreciation and understanding of these problems.

Automobile Driving↗

Adenosine triphosphatase of rat liver mitochondria: detergent solubilization of an oligomycin- and dicyclohexylcarbodiimide-sensitive form of the enzyme.

The hydrolytic activity of the ATPase bound to purified inner membrane vesicles of rat liver mitochondria can be increased threefold by washing extensively with a high ionic strength phosphate buffer. The specific ATPase activities of such phosphate-washed membranes are the highest reported to date for a mitochondrial membrane preparation (21-24 mumol of ATP hydrolyzed min-1 mg-1 in bicarbonate buffer at 37 degrees C). Deoxycholate (0.1 mg/mg of protein) extracts from these membranes a soluble, cold-stable ATPase complex which exhibits a specific activity under optimal assay conditions of 12 mumol of ATP hydrolyzed min-1 mg-1. This complex is not sedimented by centrifugation at 201000 g for 90 min, and readily passes through a 250-A Millipore filter. The ATPase activity of the soluble complex is inhibited 95% by 2.4 muM oligomycin. In addition, inhibitions of 60% or better are obtained in the presence of 1-8 muM dicyclohexylcarbodiimide, p-chloromercuribenzoate, venturicidin, and aurovertin. While a similar complex may be extracted with Triton X-100 this preparation is always lower in both specific activity and in inhibitor sensitivities than the complex extracted with deoxycholate. Detergents of the Tween and Brij series and other detergents of the Triton series are also much less effective than deoxycholate in solubilizing the oligomycin-sensitive. ATPase complex of rat liver. It is concluded that deoxycholate is superior to other detergents as an extractant of the oligomycin-sensitive ATPase complex of rat liver mitochondria, and that the complex extracted with deoxycholate possesses a closer similarity to the membrane-associated ATPase than does the complex extracted with Triton X-100. These studies document the first report of a detergent-solubilized, oligomycin-sensitive ATPase preparation from rat liver mitochondria.

Adenosine Triphosphatases↗