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  • Title: Elution of the regulatory subunit of cAMP-dependent protein kinase Type I isozyme derived from epididymal fat within the type II isozyme chromatographic peak.
    Author: Malkinson AM, Beer DS, Wehner JM, Sheppard JR.
    Journal: Biochem Biophys Res Commun; 1983 Apr 15; 112(1):214-20. PubMed ID: 6301498.
    Abstract:
    No cAMP-dependent protein kinase activity is found upon DEAE-cellulose chromatography of mouse fat extracts at the low salt concentration characteristic of the Type I isozyme. The RI detected in fat extracts by photoincorporation of the analog, 8-N3 [32P]cAMP, elutes within the high salt Type II isozyme peak. The multiple charge variants of this photolabeled RI which can be resolved by two-dimensional gel electrophoresis are similar to those of the histoptypically-related cultured cells, SV3T3 and 3T6, which do contain Type I kinase isozyme activity peaks. This high salt-eluting RI may be part of a Type I holoenzyme whose elution properties are altered by interactions with other substances present in the extract.
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