首页> 外文期刊>Journal of Molecular and Cellular Cardiology >Frank-Starling law and mass action calcium activation of the myofibril ATPase; comment on 'de Tombe PP, Mateja RD, Tachampa K, Mou YA, Farman GP, Irving TC. Myofilament length dependent activation. J Mol Cell Cardiol 2010; 48: 851-8'.
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Frank-Starling law and mass action calcium activation of the myofibril ATPase; comment on 'de Tombe PP, Mateja RD, Tachampa K, Mou YA, Farman GP, Irving TC. Myofilament length dependent activation. J Mol Cell Cardiol 2010; 48: 851-8'.

机译:弗兰克-史达琳定律和肌原纤维ATPase的钙质活化作用;关于“ de Tombe PP,Mateja RD,Tachampa K,Mou YA,Faman GP,Irving TC。肌丝长度依赖性激活。JMol Cell Cardiol 2010; 48:851-8”的评论。

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摘要

This is a question that has puzzled scientists for nearly 100 years. Earlier studies focused on biochemical and ionic mechanisms, and more recently, considerable attention has been given to structural analyses of the sarcomere as described in the review of de Tombe et al. [1 ] and other recent reviews [2,3]. Despite this considerable effort, the question remains unanswered. I suggest that one of the major limitations in thinking about this problem is the "assumption" that most workers make (and which is repeated in the review of de Tombe et al.) that the increase in Ca~(2+) sensitivity of the ATPase or contractile response is due to increased cooperativity of Ca~(2+) binding (or resulting cross-bridges) for example [1-5].
机译:这个问题困扰着科学家将近100年。较早的研究集中在生化和离子机理上,最近,如De Tombe等人的综述中所述,对肌节的结构分析给予了相当大的关注。 [1]和其他近期评论[2,3]。尽管付出了巨大的努力,但这个问题仍未得到解答。我认为,考虑该问题的主要限制之一是大多数工人做出的“假设”(并且在de Tombe等人的评论中重复了这一假设),即对Ca 2+敏感性的增加。 ATPase或收缩反应是由于Ca〜(2+)结合(或产生的跨桥)的协同作用增加而引起的,例如[1-5]。

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