TY - JOUR
T1 - Identification of the multifunctional calmodulin-dependent protein kinase in the cytosol, sarcoplasmic reticulum, and sarcolemma of rabbit skeletal muscle
AU - Sato, Hiroshi
AU - Fukunaga, Kohji
AU - Araki, Shukuro
AU - Ohtsuki, Iwao
AU - Miyamoto, Eishichi
N1 - Funding Information:
’ This research was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan (61115002) and a Grant (86-03-40) from the National Center of Neurology and Psychiatry (NCNP) from the Ministry of Health and Welfare of Japan. ’ To whom correspondence should be addressed.
PY - 1988/1
Y1 - 1988/1
N2 - A multifunctional calmodulin-dependent protein kinase (calmodulin kinase) was purified from the cytosol of rabbit skeletal muscle as a subunit of 58 kDa. A 58-kDa protein in sarcoplasmic reticulum (SR) and sarcolemma (SL) of rabbit skeletal muscle was endogenously phosphorylated in a calmodulin-dependent manner. The 58-kDa protein in SR and SL was considered to be identical to the subunit of cytosol calmodulin kinase on the basis of immunoreactivity, calmodulin binding, and autophosphorylation studies and on the patterns of protease-treated phosphopeptides. Calmodulin kinase showed broad substrate specificity and phosphorylated troponins I and T.
AB - A multifunctional calmodulin-dependent protein kinase (calmodulin kinase) was purified from the cytosol of rabbit skeletal muscle as a subunit of 58 kDa. A 58-kDa protein in sarcoplasmic reticulum (SR) and sarcolemma (SL) of rabbit skeletal muscle was endogenously phosphorylated in a calmodulin-dependent manner. The 58-kDa protein in SR and SL was considered to be identical to the subunit of cytosol calmodulin kinase on the basis of immunoreactivity, calmodulin binding, and autophosphorylation studies and on the patterns of protease-treated phosphopeptides. Calmodulin kinase showed broad substrate specificity and phosphorylated troponins I and T.
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U2 - 10.1016/0003-9861(88)90468-7
DO - 10.1016/0003-9861(88)90468-7
M3 - Article
C2 - 3341752
AN - SCOPUS:0023859070
VL - 260
SP - 443
EP - 451
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 1
ER -