scholarly journals Structure and function of fish fast skeletal muscle myosin light chains

2002 ◽  
Vol 68 (sup2) ◽  
pp. 1499-1502 ◽  
Author(s):  
SHOICHIRO ISHIZAKI ◽  
YASUYUKI MASUDA ◽  
MUNEHIKO TANAKA ◽  
SHUGO WATABE
1988 ◽  
Vol 78 (1) ◽  
pp. 65-70 ◽  
Author(s):  
Odile Cohen-Haguenauer ◽  
Paul J. R. Barton ◽  
Nguyen Van Cong ◽  
Stéphane Serero ◽  
Marie-Sylvie Gross ◽  
...  

Nature ◽  
1993 ◽  
Vol 365 (6445) ◽  
pp. 454-456 ◽  
Author(s):  
Susan Lowey ◽  
Guillermina S. Waller ◽  
Kathleen M. Trybus

1985 ◽  
Vol 11 (6) ◽  
pp. 533-540 ◽  
Author(s):  
Henryk Czosnek ◽  
Peter E. Barker ◽  
Frank H. Ruddle ◽  
Benoit Robert

1988 ◽  
Vol 16 (2-3) ◽  
pp. 227-236 ◽  
Author(s):  
Jean-Jacques Pernelle ◽  
Pier Giorgio Righetti ◽  
Juan Pedro Wahrmann

1980 ◽  
Vol 185 (1) ◽  
pp. 265-268 ◽  
Author(s):  
J Wikman-Coffelt

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.


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