Abstract
Inhibitor-2 was partially purified from rabbit liver by fractionation with ammonium sulphate, heat treatment at 100°C, precipitation with trichloroacetic acid, chromatography on DEAE-cellulose at pH 8.5 and 5.0 and gel filtration on Sephadex G-100 (Stokes radius, 3.4 nm). The protein behaved as a single component at each step and migrated on SDS-polyacrylamide gels as a 31 kDa protein. Its properties were indistinguishable from those of skeletal muscle inhibitor-2. The results disagree with the report of Khandelwal and Zinman (J. Biol. Chem. (1978) 253, 560-565) that hepatic inhibitor-2 is a 14 kDa protein.
Original language | English |
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Pages (from-to) | 155-158 |
Number of pages | 4 |
Journal | BBA - Molecular Cell Research |
Volume | 847 |
Issue number | 1 |
DOIs | |
Publication status | Published - 30 Oct 1985 |
Keywords
- (Rabbit liver)
- Inhibitor-2
- Molecular mass
- Protein phosphorylation
ASJC Scopus subject areas
- Biophysics
- Cell Biology
- Molecular Biology