Adachi K, Carruthers C A, Walsh M P
Biochem Biophys Res Commun. 1983 Sep 30;115(3):855-63. doi: 10.1016/s0006-291x(83)80013-8.
Examination, by immunoblotting, of myosin light chain kinase-containing fractions obtained during purification of the enzyme from chicken gizzard has shown that a single species (Mr = 136,000) exists in the muscle and that this enzyme is degraded, primarily to a 130,000-dalton fragment, during purification. These conclusions were confirmed by phosphorylation of the different species of myosin light chain kinase by the isolated catalytic subunit of cyclic AMP-dependent protein kinase.
通过免疫印迹法对从鸡砂囊中纯化该酶过程中获得的含肌球蛋白轻链激酶的组分进行检测，结果表明，肌肉中存在单一类型的酶（相对分子质量=136,000），并且在纯化过程中该酶主要降解为一个130,000道尔顿的片段。环磷酸腺苷依赖性蛋白激酶的分离催化亚基对不同类型的肌球蛋白轻链激酶进行磷酸化，证实了这些结论。
