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目的：研究人早幼粒白血病ＨＬ－６０细胞蛋白激酶ＣＫ２的性质。方法：经二次ＤＥ－５２离子交换纤维素柱，一次肝素－Ｓｅｐｈａｒｏｓｅ４８亲和层析柱纯化后的ＣＫ２（纯化了１３９倍，回收率为１１．８％），以［γ－３２Ｐ］ＡＴＰ和［γ－３２Ｐ］ＧＴＰ为磷酸供体，以去磷酸化酪蛋白为底物，对其性质进行研究。结果：Ｃａ２＋、ｃＡＭＰ、ｃＧＭＰ等第二信使对ＨＬ－６０细胞的ＣＫ２活性无显著影响。肝素抑制ＣＫ２活性，而精胺激活ＣＫ２，肝素与精胺对ＣＫ２的作用在一定浓度范围内呈剂量依赖性。对ＣＫ２的动力学研究测得其米氏常数Ｋｍ（ＧＴＰ）为３４．０μｍｏｌ／Ｌ。结论：ＣＫ２是一种不依赖于Ｃａ２＋、ｃＡＭＰ、ｃＧＭＰ等第二信使的蛋白激酶，肝素是其抑制剂，精胺是其激活剂。
Objective: To study the properties of protein kinase CK2 in human promyelocytic leukemia HL-60 cells. Methods: The purified CK2 was purified by secondary DE-52 ion exchange cellulose column and primary heparin-Sepharose 48 affinity column (139 times, 11.8% recovery), and purified by [γ-32P] [Γ-32P] GTP is a phosphate donor, and its properties are studied using dephosphorylated casein as a substrate. Results: The second messengers such as Ca2 +, cAMP and cGMP had no significant effect on the CK2 activity of HL-60 cells. Heparin inhibited CK2 activity, whereas spermine activated CK2. The effect of heparin and spermine on CK2 was dose-dependent at a range of concentrations. Kinetic studies of CK2 measured the Michaelis constant Km (GTP) of 34.0 μmol / L. Conclusion: CK2 is a protein kinase that is independent of the second messenger such as Ca2 +, cAMP and cGMP. Heparin is the inhibitor of CK2 and spermine is the activator of CK2.