[Epidemiologic studies after the disaster in Czernobyl in the population of children in the Krakow region]. / Badania epidemiologiczne po awarii w Czarnobylu w populacji dzieci w regionie krakowskim.

In 1989-1990 the epidemiologic studies about the impact of of Czarnobyl events on the health of children in Kraków and Nowy Sacz region were performed. The morphologic and functional changes of thyroid gland in children were estimated. Almost 90% of children in both districts received the iodine preparations for prophylactic reason. The mean time of intake was between 5-10 days following the Czarnobyl explosion. There were no relationship between the dose of iodine absorbed during prophylactic action and incidence of goiter. The prevalence of goiter amounted to 34.8-47.6% in boys and girls consecutively in Kraków district and 53.8-70.5% in Nowy Sacz. No hormonal changes in T3, T4 and TSH serum concentration were found in children with goiter and those without goiter. The complications after iodine intake were transient and seen only in a small number of children.

A fluorescence and NMR relaxation study of thermally-induced conformational changes in liver alcohol dehydrogenase.

Fluorescence and NMR relaxation studies have been performed on horse liver alcohol dehydrogenase (alcohol: NAD + oxidoreductase, EC 1.1.1.1) as a function of temperature. Observations of both the intrinsic protein fluorescence and the fluorescence of a noncovalently bound apolar probe, 2-(p-toluidinyl)naphthalene-6-sulfonic acid (TNS), indicate that a significant thermal transition occurs in the protein in the range of temperature 0-40 degrees C, and that there are different temperature-dependent forms of the enzyme. The transition between these forms is affected by the binding of specific ligands to the enzyme's active site. Time-resolved fluorescence studies of the two tryptophan residues in the enzyme suggest that this thermal transition occurs around tryptophan-314, which is buried near the intersubunit region. Binding of nucleotide to the enzyme causes a decrease in spin-lattice relaxation time, T1, which may result from a decrease in the number of water molecules bound to the protein. The observed results may be due to the interactions between the structural domains into which the monomer of the protein is folded.