Myosin light chain phosphorylation in intact human muscle |
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Authors: | M E Houston M D Lingley D S Stuart R W Grange |
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Institution: | Department of Kinesiology, University of Waterloo, Waterloo Ontario N2L 3G1, Canada |
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Abstract: | 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. |
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