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Biomedical subjects

J F Adams

Publications and source records attributed to J F Adams.

At least 37 records · Page 2Linked to original sources
PubMed1980

Time-course of formation of volatile reductive metabolites of halothane in humans and an animal model.

The time-course of the formation of 2-chloro-1,1,1-trifluoroethane (CTF) and 2-chloro-1-1-difluoroethylene (CDF), two recently identified volatile reductive metabolites of halothane, has been studied in four patients receiving 1% halothane with 99% oxygen. The concentrations of CTF and CDF in end-expired breath increased with time and reached a plateau after approximately 60 min from commencing administration. A similar time-course and plateau was seen when Fischer 344 rats were anaesthetized with halothane 1% in oxygen. However, there was an eight-fold and 12-fold increase in CTF and CDF concentrations respectively when halothane 1% was administered under conditions of mild hypoxia (oxygen 14% inspired) to rats pretreated with phenobarbitone (this results in a marked increase in serum alanine aminotransferase (ALT) and necrotic damage in the vicinity of the central veins of the liver). It is suggested that breath concentrations of CDF and CTF provide a sensitive method of monitoring the reductive metabolism of halothane.

Adult↗
PubMed1979

Hepatotoxicity and halothane metabolism in an animal model with application for human toxicity.

Centrilobular necrosis and a ten-fold elevation in serum alanine amino-transferase (ALT) consistently followed 2 hours of 1% halothane anaesthesia in an animal model. Conditional factors were the presence of enzyme induction and moderate hypoxia (14% oxygen), indicating an association between reductive metabolism and hepatotoxicity. Under these conditions there was at least a four-fold increase in reductive metabolites detected in the exhaled air. In clinical studies, reductive metabolites were also detected in the exhaled air of all patients examined, even after halothane anaesthesia with 100% oxygen. The amounts of reductive metabolites were comparable in man and the model, following equivalent halothane doses. It appears that a model with a similar route and rate of halothane biotransformation to man has been identified. The lesion of halothane hepatotoxicity in this model appears to be similar to that reported in man - centrilobular hepatic necrosis.

Alanine Transaminase↗
PubMed1977

The forms of vitamin B12 on the transcobalamins.

1. The transcobalamins from normal serum were obtained in two fractions. One contained transcobalamin I and transcobalamin III: the other contained transcobalamin II. The forms of vitamin B12 in the two fractions were then examined. 2. Methylcobalamin and adenosylcobalamin were found in both fractions. Hydroxocobalamin was found in the fraction containing transcobalamin I and transcobalamin III. Cyanocobalamin was found in both fractions in two cases, in the transcobalamin III fraction only in one case and was absent in one case.

Blood Proteins↗
PubMed1977

Conversion of hydroxo(aquo) cobalamin to sulfitocobalamin in the absence of light: a reaction of importance in the identification of the forms of vitamin B12, with possible clinical significance.

During determinations of the forms of vitamin B12 in foods and human tissues several samples yielded a growth zone on bioautography which was distinct from those due to methylcobalamin, adenosylcobalamin, hydroxocobalamin, or cyanocobalamin. The material responsible for this growth zone was identified as sulfitocobalamin and the mechanisms in its formation from hydroxocobalamin involve absence of light and the presence of bisulphite ions derived from atmospheric sulfur dioxide or indigenous sulfite ions. The formation of sulfitocobalamin during the extraction of cobalamins from foods and tissues can be prevented by reception and homogenization of the material in an ammonia buffer instead of water; the hydroxocobalamin is then converted to ammonia cobalamin, which is more resistant to attack by (bi)sulfite ions. The conversion of hydroxo(aquo)cobalamin to sulfitocobalamin in the dark can be rapid, and materials for analysis should be placed in the ammonia buffer before darkroom work is begun. The rapid conversion of hydroxo(aquo)cobalamin to sulfitocobalamin in the dark raises the possibility that hydroxocobalamin in foods may be converted to the less well absorbed sulfitocobalamin in the upper gastrointestinal tract.

Animals↗
PubMed1976

The forms of vitamin B12 in foods.

1. The forms of vitamin B12 were determined in foods, most of which had been prepared for consumption. 2. Five forms were detected: adenosylcobalamin, hydroxocobalamin, methylcobalamin, cyanocobalamin and sulphitocobalamin. Adenoxylcobalamin and hydroxocobalamin were the predominant forms. 3. The intestinal absorption of [57Co]sulphitocobalamin was estimated and found to be lower than that of [58Co]cyanocobalamin.

Adult↗
PubMed1971

Activities of various cobalamins for Euglena gracilis with reference to vitamin B 12 assay with Euglena.

Coenzyme B(12) and methylcobalamin in water are less active in promoting growth of Euglena gracilis Z strain than the same concentrations of cyanocobalamin and hydroxocobalamin which are equally active. When bound to human serum or human liver homogenate, however, the activities of these four cobalamins do not differ significantly with one exception. The results suggest that the Euglena assay using cyanocobalamin standards is not satisfactory for quantitation of coenzyme B(12) and methylcobalamin in water but acceptable when coenzyme B(12) and methylcobalamin are bound to serum or liver. Sulphitocobalamin in water is as active as cyanocobalamin and hydroxocobalamin but nitritocobalamin is less active. Factor B, the monocarboxylic acids of cyanocobalamin and hydroxocobalamin, and the dicarboxylic acid of cyanocobalamin in water were inactive.

Biological Assay↗