Characterization of multiple charge isomers of the inhibitor protein of the cyclic AMP-dependent protein kinase from bovine heart and rabbit skeletal muscle

作者: Susan Whitehouse , John M. McPherson , Donal A. Walsh

DOI: 10.1016/0003-9861(80)90233-7

关键词: Sodium dodecyl sulfateSize-exclusion chromatographyTrichloroacetic acidGel electrophoresisIsoelectric focusingCardiac muscleBiochemistryProtein kinase AChromatographyChemistryInhibitor protein

摘要: Abstract The presence of multiple forms the inhibitor cyclic AMP-dependent protein kinase has been investigated in rabbit skeletal and bovine cardiac muscle. These tissues have each fractionated by two separate procedures, one involving mild techniques, other utilizing trichloroacetic acid precipitation heating to 95 °C. proteins partially purified preparations characterized DEAE-cellulose chromatography, gel filtration, isoelectric focusing, sodium dodecyl sulfate nondenaturing electrophoresis. In tissue three charge isomers detected. Each isomer may exist apparent molecular size designated I I′ ( J. M. McPherson, S. Whitehouse, D. A. Walsh, 1979, Biochemistry 18 , 4835–4845 ). distribution between depends on purification procedure used potentially only form tissues.

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