| Literature DB >> 8463302 |
T Salehzada1, M Silhol, A M Steff, B Lebleu, C Bisbal.
Abstract
The subunit composition of RNase L, a key enzyme in the interferon system, has been characterized. RNase L was purified from human Daudi cells on a column of 2-5A-Sepharose and used to immunize Balb/c mice. A specific monoclonal antibody which recognizes a protein of 80 kDa has been isolated. This protein has been characterized and shown to be an RNA-binding protein with nuclease activity which is associated with, but distinct from, the 80-kDa 2-5A-binding protein known previously as RNase L. It is therefore proposed that the 2-5A-dependent RNase L is a complex of two distinct subunits: an 80-kDa RNA-binding protein (i.e. the catalytic subunit) and an 80-kDa 2-5A-binding protein (i.e. the regulatory subunit).Entities:
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Year: 1993 PMID: 8463302
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157