scholarly journals High molecular weight proteins in cardiac and skeletal muscle junctional sarcoplasmic reticulum vesicles bind calmodulin, are phosphorylated, and are degraded by Ca2+-activated protease.

1984 ◽  
Vol 259 (13) ◽  
pp. 8550-8557 ◽  
Author(s):  
S Seiler ◽  
A D Wegener ◽  
D D Whang ◽  
D R Hathaway ◽  
L R Jones
1988 ◽  
Vol 7 ◽  
pp. S120
Author(s):  
Hiroko Sugiura ◽  
Shinichiro Hori ◽  
Sachiko Ohtani ◽  
Tamio ^Hirabayashi ◽  
Mizuho Nakamura

1973 ◽  
Vol 72 (2) ◽  
pp. 235-242 ◽  
Author(s):  
A. M. Reuter ◽  
J. C. Hendrick ◽  
J. Sulon ◽  
P. Franchimont

ABSTRACT The percentage of LH* bound to antibodies that have been covalently bound to cellulose is diminished in the presence of LH-free human serum and sera from various species of animals. Serum fractionation studies on Sephadex G 200 show that the greatest interference comes from the proteins eluted in the void volume i. e. the high molecular weight proteins. Specifically, the gamma M globulins and the α2-macroglobulins appear to play an important role, as demonstrated by tests in which these proteins were neutralized by gamma M and α2-macroglobulin antisera.


2010 ◽  
Vol 49 (11) ◽  
pp. 1958-1962 ◽  
Author(s):  
Pierre Gans ◽  
Olivier Hamelin ◽  
Remy Sounier ◽  
Isabel Ayala ◽  
M. Asunción Durá ◽  
...  

1990 ◽  
pp. 355-359 ◽  
Author(s):  
I. B. Zbarsky ◽  
S. N. Kuzmina ◽  
T. V. Buldyaeva ◽  
T. M. Bazarnova

1999 ◽  
Vol 14 (4) ◽  
pp. 315-330 ◽  
Author(s):  
F. M. Veronese ◽  
C. Mammucari ◽  
P. Caliceti ◽  
O. Schiavon ◽  
S. Lora

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