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Isolation and structure of repressor-like proteins from the archaeon Sulfolobus solfataricus. Co-purification of RNase A with Sso7c.

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...

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Published

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Role:
Author
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

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