Myosin light chain phosphorylation in intact human muscle

FEBS Letters

Stuart, D.S.¹  Grange, R.W.¹  Houston, M.E.¹  Lingley, M.D.¹ 

[1] Department of Kinesiology, University of Waterloo, Waterloo Ontario N2L 3G1, Canada

关键词: Myosin light chain;    Contractile activity;    Myosin light chain phosphorylation;    (Human skeletal muscle);   

DOI  :  10.1016/0014-5793(87)80274-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The phosphate content of the fast (LC2F) and two slow (LC2S and LC2S¹) phosphorylatable light chains (P-light chains) in myosin isolated from biopsy samples of rested human vastus lateralis muscle averaged 0.21, 0.28 and 0.25 mol of phosphate per mol of P-light chain, respectively. Following a 10 s maximal contraction, phosphate content was increased by almost 2-fold in the fast and two slow P-light chains. After prolonged, moderate cycling activity phosphate content was only slightly increased in the three P-light chains. These data suggest that, unlike animal skeletal muscle, myosin light chain kinase and phosphatase activities are similar in human fast and slow muscle fibres.

【 授权许可】

Unknown