| Autor: |
Worrall, D.Margaret, Lambert, Sarah F., Tubbs, Philip K. |
| Zdroj: |
FEBS Letters; January 1985, Vol. 187 Issue: 2 p277-279, 3p |
| Abstrakt: |
The bifunctional enzyme CoA synthase can be nicked by trypsin without loss of its activities. The original dimer of subunit Mrapprox. 61000 yields fragments of Mr41000 and 22000 as seen on gel electrophoresis in the presence of SDS, but the nicked enzyme retains the native Mrof 118 000. Further proteolysis occurs rapidly in the absence of protecting substrates. The N-terminal of native CoA synthase is proline, and proteolysis exposes glycine as a second N-terminal. This evidence strongly suggests that the subunits are identical. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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