THE BINDING OF SMOOTH-MUSCLE MYOSIN LIGHT CHAIN KINASE TO ACTIN
THE BINDING OF SMOOTH-MUSCLE MYOSIN LIGHT CHAIN KINASE TO ACTIN
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DOI：
10.1016/s0006-291x(82)80172-1
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发表时间：
1982-01-01
影响因子：
3.1
通讯作者：
HARTSHORNE, DJ
中科院分区：
文献类型：
--
作者：
DABROWSKA, R;HINKINS, S;HARTSHORNE, DJ
从火鸡肌胆中分离的肌球蛋白L链激酶与骨骼肌肌动蛋白结合。钙离子、钙调蛋白、原肌球蛋白和镁-三磷酸腺苷的存在或不存在对结合无显著影响。随着离子强度的增加，肌球蛋白L链激酶从肌动蛋白细丝中去除。与肌动蛋白非特异性结合的可能性被认为是不太可能的，因为相互作用不受过量牛血清白蛋白的影响，而且不依赖钙的肌球蛋白L链激酶不与肌动蛋白结合。肌球蛋白L链激酶与肌球蛋白的结合不明显，在与肌动蛋白结合的条件相似的条件下，只有.apprx。有10%的肌球蛋白与肌球蛋白聚集体有关。
Myosin L chain kinase isolated from turkey gizzards binds to skeletal muscle actin. The binding was not influenced significantly by the presence or absence of Ca2+, calmodulin, gizzard tropomyosin and Mg2+-ATP. The myosin L chain kinase was removed from the actin filaments as the ionic strength was increased. The possibility of nonspecific binding to actin was considering to be unlikely since the interaction was not affected by the presence of excess bovine serum albumin and because the Ca2+-independent form of the myosin L chain kinase does not bind to actin. The binding of myosin L chain kinase to gizzard myosin was not as marked, and under conditions similar to those used to demonstrate binding to actin, only .apprx. 10% of the kinase was associated with the myosin aggregates.