Abstract
Kaempferol, 3,5,7-trihydroxy-2-(4-hydroxyphenyl)-4H-1-benzopyran-4-one, was found to inhibit bovine aorta myosin light chain kinase with a Ki of 0.3−0.5 uM . It was found to be competitive with ATP and non-competitive with isolated myosin light chains. The specificity of this inhibitor was studied relative to protein kinase C and cAMP dependent protein kinase (IC50 = 15 uM and 150 uM , respectively). It appears not to interact strongly with calmodulin binding proteins, such as Ca 2+-calmodulin dependent phosphodiesterase (IC50 - 45 uM ), and had little effect on actin-activated myosin subfragment-1 ATPase activity (IC50 > 100 uM ) or smooth muscle phosphatase activities (IC50 > 100 uM ).
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