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• W2094905898 abstract "The rate of relaxation from steady-state force in rabbit psoas fiber bundles was examined before and after phosphorylation of myosin regulatory light chain (RLC). Relaxation was initiated using diazo-2, a photolabile Ca2+ chelator that has low Ca2+ binding affinity (KCa = 4.5 × 105 M−1) before photolysis and high affinity (KCa = 1.3 × 107 M−1) after photolysis. Before phosphorylating RLC, the half-times for relaxation initiated from 0.27 ± 0.02, 0.51 ± 0.03, and 0.61 ± 0.03 Po were 90 ± 6, 140 ± 6, and 182 ± 9 ms, respectively. After phosphorylation of RLC, the half-times for relaxation from 0.36 ± 0.03 Po, 0.59 ± 0.03 Po, and 0.65 ± 0.02 Po were 197 ± 35 ms, 184 ± 35 ms, and 179 ± 22 ms. This slowing of relaxation rates from steady-state forces less than 0.50 Po was also observed when bundles of fibers were bathed with N-ethylmaleimide-modified myosin S-1, a strongly binding cross-bridge derivative of S1. These results suggest that phosphorylation of RLC slows relaxation, most likely by slowing the apparent rate of transition of cross-bridges from strongly bound (force-generating) to weakly bound (non-force-generating) states, and reduces or eliminates Ca2+ and cross-bridge activation-dependent changes in relaxation rates." @default.
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• W2094905898 date "1998-01-01" @default.
• W2094905898 modified "2023-09-27" @default.
• W2094905898 title "Phosphorylation of Myosin Regulatory Light Chain Eliminates Force-Dependent Changes in Relaxation Rates in Skeletal Muscle" @default.
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• W2094905898 doi "https://doi.org/10.1016/s0006-3495(98)77793-8" @default.
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