Phosphorylation of paramyosin.
Phosphorylation of paramyosin.
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副肌球蛋白的磷酸化。
DOI：
10.1016/0305-0491(89)90171-5
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发表时间：
1989
期刊：
影响因子：
--
通讯作者：
Hartshorne,DJ
中科院分区：
文献类型：
--
作者：
Watabe,S;Tsuchiya,T;Hartshorne,DJ
1. 用内源性激酶磷酸化了雇佣兵的肌原纤维。在一定的离子强度范围内，只有副肌凝蛋白被磷酸化。2. 副肌球蛋白的硫代磷酸化引起肌动蛋白激活的肌原纤维稳态atp酶活性的抑制。3. 有人提出内源性激酶是camp依赖性蛋白激酶的催化亚基。4. 测定了磷酸化位点周围的序列。5. 磷酸化位点可能靠近副肌球蛋白分子的c端。
1. Myofibrils isolated from Mercenaria mercenaria were phosphorylated by endogenous kinase. Over a range of ionic strengths only paramyosin was phosphorylated. 2. Thiophosphorylation of paramyosin caused an inhibition of steady-state actin-activated ATPase activity of the myofibrils. 3. It is proposed that the endogenous kinase is the catalytic subunit of the cAMP-dependent protein kinase. 4. The sequence around the phosphorylation site was determined. 5. The phosphorylation site probably is close to the C-terminus of the paramyosin molecule.