Structural evidence for three different types of glutathione transferase in human tissues

Cytosolic glutathione transferase was purified from human placenta and human liver. Three different forms of the enzyme were obtained, the acidic (pi), the near-neutral (mu), and the basic (alpha-epsilon) forms; two had free alpha-amino groups (pi, mu) and one had a blocked alpha-amino group (alpha-epsilon). N-terminal sequence analyses and total compositions gave clearly different results for each form, although transferases pi and mu showed 35% sequence homology in the N-terminal regions, with a 1-residue shift in starting position. Consequently, the proteins are concluded to be products of three discrete but related genes.     

Discrimination between duroquinol oxidase activity and the terminal oxidation step of the cyanide-resistant electron transport pathway of plant mitochondria

Comparison of the cyanide-resistant duroquinol oxidase activity of sub-mitochondrial particles from Arum maculatum L. with their ability to carry out a cyanide-resistant oxidation of NADH and succinate shows that heat-inactivation of the duroquinol oxidase activity does not proportionally affect NADH and succinate oxidation. Moreover, 1 microM antimycin inhibits duroquinol oxidase activity by 50% while not decreasing the rates of NADH and succinate oxidation. Therefore, the cyanide-resistant electron transport does not appear to be mediated by a "duroquinol oxidase", and a convincing proof of the existence of a specific protein acting as a cyanide-resistant oxidase in plant mitochondria is still lacking.     

Der Einfluß des Thioharnstoffs auf den Sauerstoffverbrauch der Fische in hypothermischen Bedingungen

Zusammenfassung Die Wirkung des in Wasser gegebenen Thioharnstoffs auf den Sauerstoffverbrauch der Fische (Carassius auratus gibelio Bloch.) wird untersucht. Die Fische waren an niedrige Temperaturen angepaßt.Der Sauerstoffverbrauch der Fische bei niedrigen Temperaturen (7–9° C) während einer 30tägigen Behandlung mit Thioharnstoff (1 g/l) erreicht eine durchschnittliche Steigerung von 61,23%.In ähnlichen Temperaturbedingungen (5–7° C) und während der gleichen Behandlungsperiode verursacht eine doppelte Thioharnstoffdosis (2 g/l) eine Steigerung des Sauerstoffverbrauchs der Fische.Der hypermetabolische Effekt des Thioharnstoffs ist schon nach den ersten drei Tagen der Behandlung deutlich; er zeigt eine beträchtliche Verminderung in den folgenden 24 Std nach dem Einstellen der Behandlung.

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The action of thiourea administered in water on the oxygen consumption of fishes in hypothermic conditions

Summary The action of thiourea administered in water on the oxygen consumption of fishes (Carassius auratus gibelio Bloch.) acclimatized to low temperatures (7–9° C) was investigated.The results of the performed experiments led to the following conclusions.At 7 to 9° C, during a thiourea treatment period of 30 days (1 g/l of water), the oxygen consumption of fishes recorded an average increase by 61.23 per cent.Under similar conditions (5–7° C) and doubling the thiourea dosis (2 g/l of water) an increase of the oxygen consumption by 158.92 per cent was stated.The hypermetabolic effect of thiourea is onsetting after the first three days of treatment and decreases significantly only after 24 hours from stopping the latter.

     

Identification of a novel glutathione transferase in human skin homologous with class alpha glutathione transferase 2-2 in the rat.

Six forms of glutathione transferase with pI values of 4.6, 5.9, 6.8, 7.1, 8.5 and 9.9 have been isolated from the cytosol fraction of normal skin from three human subjects. The three most abundant enzymes were an acidic Class Pi transferase (pI 4.6; apparent subunit Mr 23,000), a basic Class Alpha transferase (pI 8.5; apparent subunit Mr 24,000) and an even more basic glutathione transferase of Class Alpha (pI 9.9; apparent subunit Mr 26,500). The last enzyme, which was previously unknown, accounts for 10-20% of the glutathione transferase in human skin. The novel transferase showed greater similarities with rat glutathione transferase 2-2, another Class Alpha enzyme, than with any other known transferase irrespective of species. The most striking similarities included reactions with antibodies, amino acid compositions and identical N-terminal amino acid sequences (16 residues). The close relationship between the human most basic and the rat glutathione transferase 2-2 supports the classification of the transferases previously proposed and indicates that the similarities between enzymes isolated from different species are more extensive than had been assumed previously.     

Separable models for age-structured population genetics

This paper is concerned with the applications of nonlinear age-dependent dynamics to population genetics. Age-structured models are formulated for a single autosomal locus with an arbitrary number of alleles. The following cases are considered: a) haploid populations with selection and mutation; b) monoecious diploid populations with or without mutation reproducing by self-fertilization or by two types of random mating. The diploid models do not deal with selection. For these cases the genic and genotypic frequencies evolve towards time-persistent forms, whether the total population size tends towards exponential growth or not.     

Cytosolic glutathione transferases from rat liver. Primary structure of class alpha glutathione transferase 8-8 and characterization of low-abundance class Mu glutathione transferases.

Six GSH transferases with neutral/acidic isoelectric points were purified from the cytosol fraction of rat liver. Four transferases are class Mu enzymes related to the previously characterized GSH transferases 3-3, 4-4 and 6-6, as judged by structural and enzymic properties. Two additional GSH transferases are distinguished by high specific activities with 4-hydroxyalk-2-enals, toxic products of lipid peroxidation. The most abundant of these two enzymes, GSH transferase 8-8, a class Alpha enzyme, has earlier been identified in rat lung and kidney. The amino acid sequence of subunit 8 was determined and showed a typical class Alpha GSH transferase structure including an N-acetylated N-terminal methionine residue.