Властивостi позаклiтинної фруктозо-1,6-бiсфосфатази Вacillus subtilis
Extracellular fructose bisphosphatase (FBFase) (EC 3.1.3.11) from spore-forming bacterium Bacillus subtilis is obtained. The enzyme is inactivated in the absence of Mg2+ or Mn2+. Maximum activity of the enzyme is observed with substrate at the 2mM concentration. AMP inhibits FBFase activity, but...
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| Date: | 2008 |
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| Main Authors: | , , |
| Format: | Article |
| Language: | Ukrainian |
| Published: |
Видавничий дім "Академперіодика" НАН України
2008
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| Subjects: | |
| Online Access: | https://nasplib.isofts.kiev.ua/handle/123456789/3903 |
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| Journal Title: | Digital Library of Periodicals of National Academy of Sciences of Ukraine |
| Cite this: | Властивостi позаклiтинної фруктозо-1,6-бiсфосфатази Вacillus subtilis / О.В. Ястребова, Л.П. Панченко, I. Г. Скрипаль // Доп. НАН України. — 2008. — № 4. — С. 176-181. — Бібліогр.: 15 назв. — укр. |
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Digital Library of Periodicals of National Academy of Sciences of Ukraine| Summary: | Extracellular fructose bisphosphatase (FBFase) (EC 3.1.3.11) from spore-forming bacterium
Bacillus subtilis is obtained. The enzyme is inactivated in the absence of Mg2+ or Mn2+.
Maximum activity of the enzyme is observed with substrate at the 2mM concentration. AMP
inhibits FBFase activity, but the presence of PEP reduces this effect. Heavy metal ions at a
concentration of 0.1 mM in the presence of Mg2+ are not inhibitors. Effect of Zn2+ ions on the
enzyme activity is different depending on pH and the presence of Mg2+ and EDTA. Monovalent
cations are insignificant effectors of extracellular FBFase only at their low concentrations.
The subunit size determined by SDS-PAGE analysis was 63 kDa, which was confirmed by gelfiltration (230 kDa).
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| ISSN: | 1025-6415 |