| Literature DB >> 6769430 |
Abstract
The non-specific Ca2+-binding sites of skeletal-muscle myosin are located on the light chains; with the dissociation of light chains there is a corresponding decrease in the number of Ca2+-binding sites on light-chain-deficient myosin. The released light chains have a decreased binding affinity. Myosin heavy chains indirectly influence the Ca2+-binding properties of light chains by increasing the affinity of light chains for bivalent cations; this influence varies with pH. Because of light-chain dissociation at low Ca2+ and/or Mg2+ concentrations, anomalies may exist when analyses of non-specific Ca2+-binding properties of myosin are assessed by dialysis equilibrium.Entities:
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Year: 1980 PMID: 6769430 PMCID: PMC1161294 DOI: 10.1042/bj1850265
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857