兔骨骼肌肌球蛋白轻链选择性修饰的优化条件
Refined conditions for selective modifications of rabbit skeletal myosin light chains.
作者信息
Burgat J M, Roulet A, Cardinaud R
机构信息
Laboratoire de Biologie Physico-chimique, Université de Paris-Sud, Orsay, France.
出版信息
Biochimie. 1992 Dec;74(12):1083-90. doi: 10.1016/0300-9084(92)90006-z.
We selectively modified the LC1 and LC2 N-terminus as an approach to understand the function of skeletal myosin light chains and their possible implication in some diseases. Three new myosin isoforms were thus created, namely: myosin-[(P)LC1'], myosin-[(T)LC2'] and myosin-[(CT)LC2"] in which the N-terminus was selectively cleaved at Lys7 in (P)LC1', Arg8 in (T)LC2' and Phe19 in (CT)LC2". In order to obtain species with a minimum amount of secondary cleavages, eight to 12 different conditions were screened for each species and the two most efficient conditions were tested at the preparative scale.
我们选择性地修饰了LC1和LC2的N端，以此来了解骨骼肌肌球蛋白轻链的功能及其在某些疾病中的潜在影响。由此产生了三种新的肌球蛋白亚型，即：肌球蛋白 - [(P)LC1']、肌球蛋白 - [(T)LC2']和肌球蛋白 - [(CT)LC2"]，其中(P)LC1'的N端在Lys7处、(T)LC2'的N端在Arg8处以及(CT)LC2"的N端在Phe19处被选择性切割。为了获得二级切割最少的样本，对每个样本筛选了8至12种不同条件，并在制备规模下测试了两种最有效的条件。
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