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