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Myosin light chain phosphorylation in intact human muscle
Author(s) -
Houston M.E.,
Lingley M.D.,
Stuart D.S.,
Grange R.W.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80274-0
Subject(s) - myosin light chain kinase , myosin , immunoglobulin light chain , phosphate , human muscle , chemistry , phosphatase , phosphorylation , inorganic phosphate , skeletal muscle , muscle contraction , biophysics , biochemistry , biology , anatomy , antibody , immunology
The phosphate content of the fast (LC2F) and two slow (LC2S and LC2S 1 ) 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.