Proteomic profiling of giant skeletal muscle proteins

2019 ◽  
Vol 16 (3) ◽  
pp. 241-256 ◽  
Author(s):  
Sandra Murphy ◽  
Paul Dowling ◽  
Margit Zweyer ◽  
Dieter Swandulla ◽  
Kay Ohlendieck
2007 ◽  
Vol 6 (6) ◽  
pp. 2295-2303 ◽  
Author(s):  
Pingbo Zhang ◽  
Yoichi Aso ◽  
Hiroyuki Jikuya ◽  
Takahiro Kusakabe ◽  
Jae Man Lee ◽  
...  

2003 ◽  
Vol 133 (4) ◽  
pp. 1154-1157 ◽  
Author(s):  
R. J. Hunter ◽  
C. Neagoe ◽  
H. A. Järveläinen ◽  
C. R. Martin ◽  
K. O. Lindros ◽  
...  

Shock ◽  
1994 ◽  
Vol 2 (3) ◽  
pp. 171-178 ◽  
Author(s):  
Erik L. Owens ◽  
Christopher J. Lynch ◽  
Ken M. McCall ◽  
Nick D. Carter ◽  
Thomas C. Vary

1960 ◽  
Vol 38 (12) ◽  
pp. 1437-1447 ◽  
Author(s):  
J. R. Dingle ◽  
J. A. Hines

The adenosinetriphosphatase (ATPase) activities of actomyosin extracts of prerigor and postrigor cod muscle, and of myosins prepared from them by ultracentrifugation in the presence of ATP, have been measured at ionic concentration 0.1 and pH 7.3. The actomyosin ATPases were strongly activated by Mg++, while those of the myosins were suppressed by Mg++, in agreement with corresponding rabbit skeletal muscle proteins. Ca++ ion also moderately activated the actomyosin ATPases, but had little effect on the myosin ATPases. When actomyosin was precipitated by dilution in the presence of ATP and Mg++, the characteristic activation by Mg++ was lost. The myosin ATPases were very labile.


2010 ◽  
Vol 98 (3) ◽  
pp. 346a
Author(s):  
Alice W. Ward ◽  
Galina Flint ◽  
Anita E. Beck ◽  
Michael J. Bamshad ◽  
Michael Regnier

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