Action of 3 tyrphostin derivatives on casein kinase II from rat liver

  • Zhongguo Yao Li Xue Bao. 1997 Jan;18(1):56-8.
T B Kang  1 ,  C Huang ,  N C Liang
Affiliations
  • 1. Institute of Medical Biochemistry, Guangdong Medical College, Zhanjiang, China.
PMID: 10072895
Abstract

Aim: To study the action of tyrphostin on Casein Kinase (CK) II.

Methods: CK II was partially purified from rat livers by sequential DE52 and heparin-Sepharose chromatography. CK II activity was assayed by incubating CK II with dephosphorylated casein and [gamma-32P]ATP.

Results: AG34 inhibited the activity of CK II with IC50 33 (27-41) mumol.L-1. Both AG372 (121 mumol.L-1) and AG1112 (150 mumol.L-1) displayed inhibitory effects on the activity of CK II. Kinetic studies of AG34 on CK II showed that it was noncompetitive with casein and ATP.

Conclusion: AG34, AG372, and AG1112 were potent inhibitors of CK II, and the inhibitory action of AG34 was noncompetitive with casein and ATP.

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