Abstract
The effect of myosin light chain phosphorylation in skeletal muscle was investigated with respect to the binding affinity of phosphorylated and dephosphorylated heavy meromyosin (HMM) for F-actin in the absence of ATP. For phosphorylated HMM the affinity was 2.5-times weaker in the presence of Ca2+ as in its absence (HMM divalent binding sites saturated only with Mg). For dephosphorylated HMM the reverse was true, the binding being 2.4-times higher in the presence of Ca2+.
Original language | English (US) |
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Pages (from-to) | 177-180 |
Number of pages | 4 |
Journal | FEBS letters |
Volume | 210 |
Issue number | 2 |
DOIs | |
State | Published - Jan 5 1987 |
Externally published | Yes |
Keywords
- (Skeletal muscle)
- Actin binding
- Dephosphorylation
- Meromyosin
- Phosphorylation
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology