Medical examiners' seminar looked at mysteries surrounding sudden death

Medical examiners in Nova Scotia recently attended their first-ever seminar concerning the skills, challenges and techniques their jobs require. It was welcomed by the physicians, most of whom are family physicians with little training in the investigation of sudden death.     

An outdoor biophotolytic system using the cyanobacterium Anabaena cylindrica B629

The cyanobacterium Anabaena cylindrica B629 was suspended in small glass beds and incubated in a gas-tight glass vessel outdoors under a gas atmosphere comprising carbon monoxide (0.2%), acetylene (5%), oxygen (6.5%), and nitrogen. The solution phase initially contained sodium bicarbonate (10mM) at pH 7. Under these conditions the organism continuously produced hydrogen gas for over three weeks. The temperature of the culture was maintained below 30°C and minimum night temperatures were recorded. The vessel was covered by a shadecloth, which reduced the natural illumination by approximately 70%. The system is an alternative to those requiring the strict absence of oxygen and little nitrogen, and requires virtually no attention during the incubation period.     

A new family of 2-hydroxyacid dehydrogenases

The NADH-dependent hydroxypyruvate reductase from cucumber and the pdxB gene product of E. coli display significant homology to E. coli D-3-phosphoglycerate dehydrogenase. In contrast, these proteins do not display much similarity with other oxidoreductases or with other 2-hydroxyacid dehydrogenases in particular. On the basis of their relatedness and the structure of their substrates, these three enzymes constitute a new family of 2-hydroxyacid dehydrogenases distinct from malate and lactate dehydrogenase.     

Varieties of Anomalous Experience: Examining the Scientific Evidence

Varieties of Anomalous Experience: Examining the Scientific Evidence. Etzel Cardeña. Steven Jay Lynn. and Stanley Krippner. eds. Washington, DC: American Psychological Association, 2000. 476 pp.     

Comparison of the precursor and mature forms of rat heart mitochondrial malate dehydrogenase

The complete amino acid sequence of mitochondrial malate dehydrogenase from rat heart has been determined by chemical methods. Peptides used in this study were purified after digestions with cyanogen bromide, trypsin, endoproteinase Lys C, and staphylococcal protease V-8. The amino acid sequence of this mature enzyme is compared with that of the precursor form, which includes the primary structure of the transit peptide. The transit peptide is required for incorporation into mitochondria and appears to be homologous to the NH2-terminal arm of a related cytoplasmic enzyme, pig heart lactate dehydrogenase. The amino acid differences between the rat heart and pig heart mitochondrial malate dehydrogenases are analyzed in terms of the three-dimensional structure of the latter. Only 12/314 differences are found; most are conservative changes, and all are on or near the surface of the enzyme. We propose that the transit peptide is located on the surface of the mitochondrial malate dehydrogenase precursor.