FEBS Letters | |
Myosin light chain phosphorylation in intact human muscle | |
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
【 预 览 】
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