PubMed · 14793506
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H H DALE. 1950. Professor E. D. Adrian.. https://doi.org/10.1016/0013-4694(50)90074-5
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BACKGROUND: Patients with advanced cancer may present complex sets of symptoms, of which pain is the most prevalent. In addition to systemic pharmacological therapy for pain management, neurolytic blocks are also effective in controlling cancer pain in selected patients. METHOD: Various neurolytic blocks used in the treatment of cancer pain are reviewed. RESULTS: Several studies have documented the efficacy of neurolytic blocks in reducing pain intensity and opioid consumption, although good prospective, randomized controlled trials are scarce. The narrow risk-benefit ratio associated with neurolysis techniques requires knowledge of the complications associated with the different neurolytic blocks in order to minimise undesirable effects. INTERPRETATION: Interventional techniques continue to play an important role in the management of cancer pain. The quality of the neurolytic blocks improves when they are performed image-guided in collaboration with an interventional radiologist. These blocks should never be considered an isolated treatment, but as a component of a comprehensive therapeutic strategy.
There has been an extensive discussion in the forensic toxicology community regarding the effect of trauma on the enzymatic method for ethanol analysis. There is a paucity of information in the literature that addresses this question. This study was designed to compare the Dade Behring Dimension enzymatic method with the reliable gas chromatographic method. The blood samples collected at the same time from trauma patients were analyzed by both methods. The result of the study shows no significant quantitative difference between the enzymatic and gas liquid chromatographic (GLC) methods. Also, the enzymatic method did not show any false positive ethanol in cases where the GLC method showed a negative finding.
Several assays for gamma-hydroxybutyrate (4-hydroxybutyrate, GHB) have been developed based on the enzyme gamma-hydroxybutyrate dehydrogenase (GHB-DH). Enzymatic oxidation of GHB by NAD+ is coupled to diaphorase-mediated reduction of pro-dye to yield colored product. GHB-DH from Ralstonia eutropha was cloned and expressed as a stable fusion protein easily purified by affinity chromatography. Quantitative initial velocity and endpoint versions of the assay in solution are described. Michaelis-Menten parameters for oxidation of GHB and ethanol were estimated. A semi-quantitative "dipstick" version of the assay on paper also is described. Both solution endpoint and "dipstick" assays are sensitive to about 0.05 mg GHB/mL using 10 microL of sample. Ethanol at concentrations possible in urine and agents used to stabilize physiological fluids for forensics analysis do not interfere significantly. The "dipstick" assay also allows detection of GHB in alcoholic beverages after evaporation of about one-fourth drop of beverage before testing. The enzymatic assay for GHB is reliable, sensitive, inexpensive and rapid.