Molecular mass of inhibitor-2 from rabbit liver

Alexander A. Chisholm, Philip Cohen

    Research output: Contribution to journalArticlepeer-review

    3 Citations (Scopus)


    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 languageEnglish
    Pages (from-to)155-158
    Number of pages4
    JournalBBA - Molecular Cell Research
    Issue number1
    Publication statusPublished - 30 Oct 1985


    • (Rabbit liver)
    • Inhibitor-2
    • Molecular mass
    • Protein phosphorylation

    ASJC Scopus subject areas

    • Biophysics
    • Cell Biology
    • Molecular Biology


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