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鸡肫肌球蛋白的P轻链磷酸化与ATP酶的肌动蛋白激活之间的非相关性。

Non-correlation of phosphorylation of the P-light chain and the actin activation of the ATPase of chicken gizzard myosin.

作者信息

Cole H A, Grand R J, Perry S V

出版信息

Biochem J. 1982 Aug 15;206(2):319-28. doi: 10.1042/bj2060319.

DOI:10.1042/bj2060319
PMID:6128971
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1158588/
Abstract
  1. The enzymic properties of myosin isolated from chicken gizzard by three different methods have been compared. 2. Although the specific Ca2+-stimulated ATPases of all preparations were similar and high, there were significant differences in the specific activities of the Mg2+-stimulated actomyosin ATPases. 3. There was no direct correlation between the Mg2+-stimulated actomyosin ATPase activity and the extent of P-light-chain phosphorylation in any of the three myosin preparations. 4. A fraction that activates the Mg2+-stimulated actomyosin ATPase of gizzard muscle has been isolated from a gizzard muscle filament preparation. 5. The activator was specific for the Mg2+-activated actomyosin ATPase of smooth muscle. 6. The activator required the addition of calmodulin for full effect.
摘要
  1. 对通过三种不同方法从鸡胗中分离出的肌球蛋白的酶学性质进行了比较。2. 尽管所有制剂的特定Ca2+刺激的ATP酶相似且活性高,但Mg2+刺激的肌动球蛋白ATP酶的比活性存在显著差异。3. 在三种肌球蛋白制剂中的任何一种中,Mg2+刺激的肌动球蛋白ATP酶活性与P轻链磷酸化程度之间均无直接相关性。4. 已从鸡胗肌丝制剂中分离出一种可激活鸡胗肌Mg2+刺激的肌动球蛋白ATP酶的组分。5. 该激活剂对平滑肌的Mg2+激活的肌动球蛋白ATP酶具有特异性。6. 该激活剂需要添加钙调蛋白才能发挥充分作用。
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fc5/1158588/e95891f628d0/biochemj00368-0137-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fc5/1158588/e95891f628d0/biochemj00368-0137-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fc5/1158588/e95891f628d0/biochemj00368-0137-a.jpg

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Non-correlation of phosphorylation of the P-light chain and the actin activation of the ATPase of chicken gizzard myosin.鸡肫肌球蛋白的P轻链磷酸化与ATP酶的肌动蛋白激活之间的非相关性。
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引用本文的文献

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2
Ca2+ can affect Vmax without changes in myosin light chain phosphorylation in smooth muscle.钙离子可在不改变平滑肌肌球蛋白轻链磷酸化的情况下影响最大反应速度。
Pflugers Arch. 1984 Aug;401(4):385-90. doi: 10.1007/BF00584340.
3
Skinned smooth muscle: calcium-calmodulin activation independent of myosin phosphorylation.

本文引用的文献

1
Contraction in intact pig aortic strips is not always associated with phosphorylation of myosin light chains.完整猪主动脉条的收缩并不总是与肌球蛋白轻链的磷酸化相关。
Biochem J. 1980 Dec 15;192(3):967-70. doi: 10.1042/bj1920967.
2
Myosin filaments have non-phosphorylated light chains in relaxed smooth muscle.在舒张状态的平滑肌中,肌球蛋白丝含有非磷酸化轻链。
Nature. 1981 Dec 10;294(5841):567-9. doi: 10.1038/294567a0.
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Phosphorylation of the calcium ion-regulated thin filaments from vascular smooth muscle. A new regulatory mechanism?
Pflugers Arch. 1986 Nov;407(5):569-71. doi: 10.1007/BF00657520.
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Study of the phosphorylatable light chains of skeletal and gizzard myosins by nuclear magnetic resonance spectroscopy.利用核磁共振光谱法对骨骼肌和肌胃肌球蛋白的可磷酸化轻链进行研究。
Biochem J. 1988 Aug 15;254(1):277-86. doi: 10.1042/bj2540277.
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Calcium-independent contraction in lysed cell models of teleost retinal cones: activation by unregulated myosin light chain kinase or high magnesium and loss of cAMP inhibition.硬骨鱼视网膜视锥细胞裂解细胞模型中的钙非依赖性收缩:由未受调控的肌球蛋白轻链激酶或高镁激活以及环磷酸腺苷抑制作用的丧失。
J Cell Biol. 1987 Jul;105(1):397-402. doi: 10.1083/jcb.105.1.397.
血管平滑肌中钙离子调节的细肌丝的磷酸化。一种新的调节机制?
Biochem J. 1981 Jul 1;197(1):127-39. doi: 10.1042/bj1970127.
4
Effect of phosphorylation on the actin-activated ATPase activity of myosin.
Biochem Biophys Res Commun. 1981 Feb 12;98(3):800-5. doi: 10.1016/0006-291x(81)91182-7.
5
The phosphorylated L2 light chain of skeletal myosin is a modifier of the actomyosin ATPase.骨骼肌肌球蛋白的磷酸化L2轻链是肌动球蛋白ATP酶的一种修饰因子。
J Biol Chem. 1980 Sep 25;255(18):8836-41.
6
Calcium ion-regulated thin filaments from vascular smooth muscle.来自血管平滑肌的钙离子调节细肌丝。
Biochem J. 1980 Feb 1;185(2):355-65. doi: 10.1042/bj1850355.
7
The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定分子量的可靠性。
J Biol Chem. 1969 Aug 25;244(16):4406-12.
8
A phosphorylated light-chain component of myosin from skeletal muscle.来自骨骼肌的肌球蛋白的一种磷酸化轻链组分。
Biochem J. 1973 Sep;135(1):151-64. doi: 10.1042/bj1350151.
9
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