Spectral changes resulting from the interaction of some N-alkyl nitrosamines and rat liver microsomes

Summary Dimethyl (DMN) and diethyl nitrosamine (DEN) do not give characteristic spectral changes upon interaction with rat liver microsomes, while dipropyl (DPN) and dibutyl (DBN) nitrosamine cause type I spectral changes. The spectral binding constant is 100 mM for DPN and 1.17 mM for DBN. The maximal spectral change is 3.2×10⁶ and 1.0×10⁶ absorbance units per milligram protein for DPN and DBN respectively.Acknowledgment. This work was supported by Grants AM 13195-07 from the National Institute of Health (USA) and from the Consejo Nacional de Investigaciones Cientificas y Técnicas (Argentina).     

Action de la capsicine sur la multiplication et la virulence de l'Agrobacterium tumefaciens

Summary It was established that the treatment of liquid cultures ofAgrobacterium tumefaciens with capsicine (in doses of 0.0025–0.01) in the course of 6 h, causes a more abundant and quicker multiplication of the micro-organism and an increase of its virulence, as measured by the method ofBernaerts andDe Ley.     

Activity of orotate metabolizing enzyme complex and various urea-cycle enzymes in mutant mice with ornithine transcarbamylase deficiency

Summary The overall activity of the enzyme complex consisting of orotate phosphoribosyl transferase and orotidine monophosphate decarboxylase, and of various enzymes of the urea cycle, has been studied in sparse-fur (spf) mutant mice with ornithine transcarbamylase deficiency. The enzyme complex has a lower overall activity, which could be caused by disturbed pyrimidine metabolism due to hyperammonemia. Other enzymes of the urea cycle do not show any significant change.Acknowledgments. The research was supported by a grant from the Conseil des Clubs Sociaux and Fondation Justine Lacoste Beaubien, Montréal. The authors wish to thank Ms Louise Poulin and Ms Francine Poisson for technical assistance.     

Comparison of the localization of several muscle proteins in relaxed and contracted myofibrils.

The localization of several muscle proteins in relaxed and contracted myofibrils is compared. The morphology of the myofibrils and the behavior of these proteins was also investigated under extraction conditions.