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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Pires E M, Perry S V

Biochem J. 1977 Oct 1;167(1):137-46. doi: 10.1042/bj1670137.

A procedure is described for the isolation of myosin light-chain kinase from rabbit fast skeletal muscle as a homogeneous protein. 2. Myosin light-chain kinase is a monomeric enzyme of mol.wt. 77000. Under some conditions of storage it is converted into components of mol.wts. about 50000 and 30000 that possess enzymic activity. 3. The enzyme is clearly different in structure and properties from any other protein kinase so far isolated from muscle. 4. The enzyme is highly specific for the P-light chain (18000-20000-dalton light chain) of myosin and requires Ca2+ for activity. 5. The P-light chain is phosphorylated at a similar rate whether isolated or associated with the rest of the myosin molecule. 6. The effects of pH, bivalent cation and other nucleotides on the enzymic activity are described. 7. The role of the phosphorylation of the P-light chain of myosin in muscle function is discussed.

本文描述了一种从兔快肌骨骼肌中分离出肌球蛋白轻链激酶的方法，该激酶为一种均一的蛋白质。2. 肌球蛋白轻链激酶是一种分子量为77000的单体酶。在某些储存条件下，它会转化为分子量约为50000和30000且具有酶活性的组分。3. 该酶在结构和性质上与迄今从肌肉中分离出的任何其他蛋白激酶明显不同。4. 该酶对肌球蛋白的磷酸化轻链（18000 - 20000道尔顿轻链）具有高度特异性，且活性需要Ca2+。5. 无论磷酸化轻链是分离的还是与肌球蛋白分子的其余部分结合，其磷酸化速率相似。6. 描述了pH、二价阳离子和其他核苷酸对酶活性的影响。7. 讨论了肌球蛋白磷酸化轻链在肌肉功能中的作用。

Pires E M, Perry S V

Biochem J. 1977 Oct 1;167(1):137-46. doi: 10.1042/bj1670137.

A procedure is described for the isolation of myosin light-chain kinase from rabbit fast skeletal muscle as a homogeneous protein. 2. Myosin light-chain kinase is a monomeric enzyme of mol.wt. 77000. Under some conditions of storage it is converted into components of mol.wts. about 50000 and 30000 that possess enzymic activity. 3. The enzyme is clearly different in structure and properties from any other protein kinase so far isolated from muscle. 4. The enzyme is highly specific for the P-light chain (18000-20000-dalton light chain) of myosin and requires Ca2+ for activity. 5. The P-light chain is phosphorylated at a similar rate whether isolated or associated with the rest of the myosin molecule. 6. The effects of pH, bivalent cation and other nucleotides on the enzymic activity are described. 7. The role of the phosphorylation of the P-light chain of myosin in muscle function is discussed.

本文描述了一种从兔快肌骨骼肌中分离出肌球蛋白轻链激酶的方法，该激酶为一种均一的蛋白质。2. 肌球蛋白轻链激酶是一种分子量为77000的单体酶。在某些储存条件下，它会转化为分子量约为50000和30000且具有酶活性的组分。3. 该酶在结构和性质上与迄今从肌肉中分离出的任何其他蛋白激酶明显不同。4. 该酶对肌球蛋白的磷酸化轻链（18000 - 20000道尔顿轻链）具有高度特异性，且活性需要Ca2+。5. 无论磷酸化轻链是分离的还是与肌球蛋白分子的其余部分结合，其磷酸化速率相似。6. 描述了pH、二价阳离子和其他核苷酸对酶活性的影响。7. 讨论了肌球蛋白磷酸化轻链在肌肉功能中的作用。