Ultrastructural characteristics of mycobacterial growth.
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Biomedical subjects
Publications and source records attributed to M Rieber.
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A study of the subcellular localization of the nicotinamide adenine dinucleotide (NADH)-3-(4, 3-dimethylthiazolyl-2)-2,5-diphenyltetrazolium bromide (MTT) oxido-reductase systems in Mycobacterium was presented. Evidence based on starch gel electrophoresis and different responses of the subcellular fractions to heat inactivation suggested the existence of more than one enzyme responsible for the NADH-MTT oxido-reductase activity. One type of activity was found in the membrane-mesosome fraction which contained labile and electrophoretically non-migrating enzymes. Another type of activity was also detected in the soluble fraction which on starch gel electrophoresis exhibited 4 bands of activity, two of which showed heat resistance.
Bacitracin-treated mycobacteria liberated tubules and phagelike particles which had no biological activity against selected species. These structures may reflect a state of defective lysogeny.
Mitomycin C has been found to stimulate the production of long-tailed defective bacteriophages and poly tails in thick cell wall mycobacterial mutants.
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1. Ribosomal preparations from dormant seed, cotyledon and growing tissue from Pisum arvense were examined. 2. Polysomes were obtained from growing tissues under all conditions used. 3. Such particles were obtained from seed immediately after imbibition only when 5mm-zinc sulphate was included in the medium used for extraction. 4. No polysomes were obtained from dry seed. 5. Extracts of dry seed showed limited incorporation of phenylalanine into protein. 6. Extracts of seed after imbibition showed enhanced activity in incorporation of phenylalanine amounting to 72% of the activity found in extracts of growing tissue. 7. A nuclear fraction from dry seed was able to incorporate ATP into acid-precipitable material. 8. It is concluded that the protein-synthesizing system of the dry seed is limited by the low concentration of functional polysomes.
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