Chisholm A A, Cohen P
Biochim Biophys Acta. 1985 Oct 30;847(1):155-8. doi: 10.1016/0167-4889(85)90168-5.
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.
通过硫酸铵分级分离、100℃热处理、三氯乙酸沉淀、在pH 8.5和5.0条件下进行DEAE - 纤维素柱层析以及Sephadex G - 100凝胶过滤(斯托克斯半径为3.4纳米),从兔肝脏中部分纯化出抑制剂 - 2。该蛋白质在每一步骤中均表现为单一成分,在SDS - 聚丙烯酰胺凝胶上迁移为一条31 kDa的蛋白质条带。其特性与骨骼肌抑制剂 - 2的特性无法区分。这些结果与Khandelwal和Zinman的报告(《生物化学杂志》(1978年)253卷,560 - 565页)不一致,该报告称肝脏抑制剂 - 2是一种14 kDa的蛋白质。