Localization of L-asparaginase inEscherichia coli |
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| Authors: | S ?trbáňová-Ne?inová O Svobodová J Vránová |
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| Institution: | (1) Department of Technical Microbiology, Institute of Microbiology, Czechoslovak Academy of Sciences, 142 20 Prague 4;(2) Institute of Hygiene and Epidemiology, Prague 10;(3) Present address: Department of Medical Microbiology and Immunology, Charles University, Prague 2 |
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| Abstract: | 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. |
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