Autor: |
T A, Shamolina, V K, Svedas |
Rok vydání: |
2000 |
Předmět: |
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Zdroj: |
Biochemistry. Biokhimiia. 65(6) |
ISSN: |
0006-2979 |
Popis: |
Individual subunits of penicillin acylase from E. coli were isolated by gel-filtration under denaturing conditions (8 M urea). Recovery of the catalytic activity of the penicillin acylase heterodimer was studied after removal of urea. In the case of the heterodimer, 40-60% of the initial activity was recovered, whereas the activity of individual subunits was not recovered. Combination of native enzyme subunits with subunits isolated from the enzyme pre-inactivated with the irreversible inhibitor phenylmethylsulfonyl fluoride resulted in heterodimers which were active only in the case of involvement of the beta-subunit of the active enzyme. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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