AIM:To study preliminarily the properties of myosin lightchain kinase(MLCK)in rabbit liver.METHODS:The expression of MLCK was detected byreverse transcdption-polymerase chain reaction(RT-PCR);the MLCK was obtained from rabbit liver,and its activitywas analyzed by γ-32p incorporation technique to detect thephosphorylation of myosin light chain.RESULTS:MLCK was expressed in rabbit liver,and theactivity of the enzyme was similar to rabbit smooth muscleMLCK,and calmodulin-dependent.When the concentrationwas 0.65 mg·L-1,the activity was at the highest level.CONCLUSION:MLCK expressed in rabbit liver may catalyzethe phosphorylation of myosin light chain,which may playimportant rolos in the regulation of hepatic cell functions.