Abstract
The changes in F-actin conformation in myosin-free single ghost fiber induced by the binding of heavy meromyosin (HMM) with dephosphorylated or phosphorylated light chains-2 (LC2) have been studied by measuring intrinsic tryptophan polarized fluorescence of F-actin. It has been found that at low concentrations of Ca2+ (pCa ≥ 8), the binding of HMM with dephosphorylated LC2 to F-actin in ghost fibres increases, whereas the binding of HMM with phosphorylated LC2 decreases the anisotropy of polarized tryptophan fluorescence. The effect is reversed at high concentrations of Ca2+ (pCa = 5). It has been assumed that this effect of myosin light chain phosphorylation may be due to its influence on the type of myosin head binding to F-actin.
Original language | English (US) |
---|---|
Pages (from-to) | 691-694 |
Number of pages | 4 |
Journal | Biokhimiya |
Volume | 51 |
Issue number | 4 |
State | Published - Jan 1 1986 |
Externally published | Yes |
ASJC Scopus subject areas
- Chemistry(all)