Heterochromatin distribution and chiasma localization in the grasshopper Bryodema tuberculata (fabr.) (Acrididae)

The problem of extreme localisation of chiasmata in the grasshopper species Bryodema tuberculata has been reinvestigated, using C-banding, Q-banding and benzimidazol techniques. These techniques reveal the precise localisation of heterochromatin in different chromosomes. Single or double heterochromatic blocks are present near the centromeric regions, except in chromosomes 5 and 11, which have larger blocks. These two chromosomes possess a distal chiasma while the other autosomes have a proximal chiasma. The results with regard to the distribution of chiasmata, in relation to the localisation of heterochromatin, as well as the existence of a short arm, are compared with the earlier observations of White, and discussed briefly.     

Localization of L-asparaginase inEscherichia coli

The localization ofl-asparaginase (l-asparagine amidohydrolase, EC 3.5.1.1) EC-2 isoenzyme was studied inEscherichia coli ATCC 9637 grown under conditions of moderate aeration. The enzyme was determined in cell fractions obtained by fraction centrifugation of lysed spheroplasts. When the synthesis of the enzyme was induced byl-asparagine, its amount in the cytoplasmic fraction at the beginning of the induction exceeded as much as five times that in uninduced cells, attaining up to 20% of the total activity. In the course of growth of the culture this activity decreased gradually to zero. The membrane fraction of induced cells contained considerable amount of EC-2l-asparaginase which, at the beginning of the induction, reached up to 6% ot the total enzymic activity; in membrane fraction of control cells the activity was close to zero. The results indicate a relationship of cell structures to thel-asparagine-induced synthesis of the enzyme.     

The influence of tetrathionate respiration on catabolite repression inCitrobacter

Anaerobic reversal of catabolite repression was partially eliminated if tetrathionate was reduced to thiosulphate.