-transparent.png){kind=logo}
Purified alpha-actinin from human platelets was digested with Ca2+-activated protease from muscle. The alpha subunit (Mr = 100 kDa) was degraded into a unique polypeptide b of slightly lower molecular mass. In fresh platelets, only the a subunit was detected by immunoblotting techniques, while in out-dated platelets, both a and b polypeptides were present. Since a similar conversion of a to b occurs in vitro as in whole platelets, it can be assumed that, in platelets, alpha-actinin is cleaved by the endogenous Ca2+-activated protease.
Related Publications
Y Gache, and
F Landon, and
H Touitou, and
A Olomucki
June 1975,
The Journal of biological chemistry,
Y Gache, and
F Landon, and
H Touitou, and
A Olomucki
March 1983,
The Biochemical journal,
Y Gache, and
F Landon, and
H Touitou, and
A Olomucki
June 1982,
Rinsho byori. The Japanese journal of clinical pathology,
Y Gache, and
F Landon, and
H Touitou, and
A Olomucki
July 1981,
Journal of biochemistry,
Y Gache, and
F Landon, and
H Touitou, and
A Olomucki
April 1982,
FEBS letters,
Y Gache, and
F Landon, and
H Touitou, and
A Olomucki
January 1983,
Methods in enzymology,
Y Gache, and
F Landon, and
H Touitou, and
A Olomucki
March 1988,
Journal of bacteriology,
Y Gache, and
F Landon, and
H Touitou, and
A Olomucki
October 1983,
Thrombosis research,
Y Gache, and
F Landon, and
H Touitou, and
A Olomucki
July 1985,
FEBS letters,
Y Gache, and
F Landon, and
H Touitou, and
A Olomucki
July 1983,
The Journal of biological chemistry,
