- Abstract:
-
The thermostable histone-like protein Sso7c (Sso for Sulfolobus solfataricus) from the archaeon Sulfolobus solfataricus was purified from the supernatant of acid-soluble cell lysates. Reverse phase HPLC of an apparently homogeneous Sso7c protein fraction from Mono S chromatography resulted in resolution of three further peaks. Sequence analysis revealed one of these components to be bovine RNase A, originating from the culture medium and explaining the RNA hydrolyzing activities of Sso7 prepa...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1016/s0014-5793(98)00848-5
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- Journal:
- FEBS letters
- Volume:
- 432
- Issue:
- 3
- Pages:
- 141-144
- Publication date:
- 1998-08-05
- DOI:
- EISSN:
-
1873-3468
- ISSN:
-
0014-5793
- URN:
-
uuid:56ac54a5-1ba0-4fea-acb8-ad62df0c7c76
- Source identifiers:
-
108686
- Local pid:
- pubs:108686
- Copyright date:
- 1998
Journal article
Isolation and structure of repressor-like proteins from the archaeon Sulfolobus solfataricus. Co-purification of RNase A with Sso7c.
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