TOXIGENIC BACTERIAL PROTEASES AND THEIR INHIBITORS - Kotb, Essam
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Among 128 proteolytic bacterial isolates, Brevibacterium otitidis, CBS-76 was choosen on the basis of secreted protease. Analysis of purified protease revealed an apparent molecular weight of 47 KDa with 15.2% glutamic acid content. The purified protease showed the maximum activity after 68h at 35ºC and pH 7.2. The purified enzyme was inhibited in the presence of EDTA but maximally activated in the presence of sodium arsenate. LD50 on mice was 8 mig /100 g body weight. Histological study using transmission electron microscope revealed that nuclei of treated mice hepatocytes appeared with…mehr

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Produktbeschreibung
Among 128 proteolytic bacterial isolates, Brevibacterium otitidis, CBS-76 was choosen on the basis of secreted protease. Analysis of purified protease revealed an apparent molecular weight of 47 KDa with 15.2% glutamic acid content. The purified protease showed the maximum activity after 68h at 35ºC and pH 7.2. The purified enzyme was inhibited in the presence of EDTA but maximally activated in the presence of sodium arsenate. LD50 on mice was 8 mig /100 g body weight. Histological study using transmission electron microscope revealed that nuclei of treated mice hepatocytes appeared with inactive heterochromatin and the nucleoli tend to disintegrate. While the cytoplasm contains swollen mitochondria and some destructed mitochondria lost their inner cristae. And fat droplets accumulated in the cytoplasm in the form of empty vacuoles(steatosis). On studying, novel inhibitors derived from common drugs derivatives of saccharin sodium,compound 6 and 9 showed the maximum percentage of enzyme inhibition.
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Autorenporträt
Dr/ Essam Kotb is a Lecturer and Researcher of Microbiology at the Faculty of Science, Zagazig University, Zagazig, Egypt. Mainly interested in proteolysis and fibrinolysis actions by bacteria.