| Autor: |
L, Váchová, H, Kucerová, J, Benesová, J, Chaloupka |
| Rok vydání: |
1994 |
| Předmět: |
|
| Zdroj: |
Biochemistry and molecular biology international. 32(6) |
| ISSN: |
1039-9712 |
| Popis: |
The intracellular Ca(2+)-dependent serine proteinase (ISP1) activity in the cytoplasm of nongrowing Bacillus megaterium incubated in a sporulation medium was determined at 35 degrees C and at temperatures decreasing the sporulation frequency (42 degrees C) or suppressing sporulation (43.5 degrees C). The enzyme in the crude cytoplasmic fraction was partially inhibited by a loosely bound inhibitor(s) because the ISP1 activity rose after protein fractionation by HPLC. Temperature shift-up or osmotic stress applied at 35 degrees C increased the development of the ISP1 activity several times. The increase was caused at least partially by the synthesis of the enzyme protein, as proved by SDS-PAGE and immunoblotting of the cytoplasm. This enzyme thus probably belongs among heat-shock proteins. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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