Tchernobyl : le vrai, le probable et le faux

The Japanese earthquake and tsunami drew attention worldwide to nuclear power plant accidents and associated health risks. Since Chernobyl 25 years ago, several studies were published and we now have precise information concerning the long-term health of the population living near nuclear power plants and also in different European countries. The authors hope to bring some answers to the key questions from the public concerning radioactive units used and their significance, the evaluation of the number of radio-induced cancers within the different countries of Europe, other eventual health effects and the problem of possible congenital anomalies. Finally, French public perception on nuclear risk is examined and the feedback of the Japanese experience is evoked.     

Distribution de la Phosphonates dans le Sang et le Sperme de Boeuf

A new assay for aminopeptidase P was established by coupling with proline iminopeptidase using Gly-Pro-chromogen (e.g. Gly-Pro-β-naphthylamide, Gly-Pro-p-nitroanilide, or .Gly-Pro-4-methyl coumarin amide) as the substrate. With each substrate, a linear relationship was established between the enzyme amounts and color development or fluorescence due to the chromogen released. This assay method did not suffer from interference by materials in culture broth. By using this assay method, aminopeptidase P was partially purified from Escherichia coli HB101 by chromatographies on DEAE-Sephadex and high performance liquid chromatography (HPLC). On the chromatogram with a DEAE-Sephadex column, two peaks of aminopeptidase P were observed and were named APP-I and APP-II. APP-I was further purified by HPLC using DEAE-5PW and Phenyl-5PW columns. Optimum pHs of APP-I and APP-II were 8.0 and 9.0, respectively. In contrast to APP-I which was stable around pH 10, APP-II was stable at pH 8 to 9. After incubation for 30 min at pH 8.0, fifty percent of the remaining activity of APP-I and APP-II were observed at 60°C and 50°C. APP-I and APP-II were activated 3-fold by the addition of 5 and 30 μm Mn²⁺. They were inhibited by EDTA, and reactivated by adding Mn^{2 +}. The molecular weights of APP-I and APP-II were 350,000 and 210,000, respectively. Each enzymes released the amino terminal amino acid when proline is at the penultimate position. The velocity of hydrolysis by the enzymes was not significantly different for most X-Pro bonds (X = amino acid) of peptides except for Pro-Pro bond. APP-II hydrolyzed penta-(Pro-Pro-Gly) at a much higher rate than APP-I, suggesting the aminopeptidase P reported by Yaron and Mlynar (BBRC, 32, 658 (1968)) to be APP-II.     

L'homme et le Langage

Sans résumé     

Synthesis and secretion of kidney beta-galactosidase in mutant le/le mice.

We have found that the pigmentation mutant light ear in the mouse has a striking effect on lysosomes in the kidney. Male mice homozygous for the le mutant allele have a 4-fold elevated concentration of kidney beta-galactosidase (EC 3.2.1.23). The abnormal elevation of kidney beta-galactosidase is the net result of two processes. First, beta-galactosidase is elevated due to the defective urinary secretion of lysosomal enzymes which is a specific effect of the le mutation. Secondly, this effect is most evident in males and testosterone-treated females because of the induction of beta-galactosidase synthesis by testosterone, which occurs in +/+ as well as in mutant mice. The pale-ear mutation (ep) which mimics the pigmentation phenotype of le also has a similar effect on kidney lysosomes.