Molecular mass of inhibitor-2 from rabbit liver.
Inhibitor-2 was partially purified from rabbit liver by fractionation with ammonium sulphate, heat treatment at 100 degrees 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.
D000645:Ammonium Sulfate; D000818:Animals; D055598:Chemical Phenomena; D011232:Chemical Precipitation; D002627:Chemistry, Physical; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D008099:Liver / Q000032:analysis*; D008970:Molecular Weight; D009132:Muscles / Q000032:analysis; D011506:Proteins / Q000302:isolation & purification*; D011817:Rabbits; D000097847:Protein Phosphatase Inhibitory Proteins
D000645:Ammonium Sulfate; D011506:Proteins; C024833:protein phosphatase inhibitor-2; D000097847:Protein Phosphatase Inhibitory Proteins