Calpain proteolysis of free and bound forms of calponin, a troponin T‐like protein in smooth muscle
Calpain proteolysis of free and bound forms of calponin, a troponin T‐like protein in smooth muscle
复制标题
钙蛋白酶对游离和结合形式的钙调蛋白(平滑肌中的肌钙蛋白 T 样蛋白)的水解作用
DOI:
10.1016/0014-5793(89)80783-5
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发表时间:
1989
期刊:
影响因子:
3.5
通讯作者:
T. Murachi
中科院分区:
文献类型:
--
作者:
S. Tsunekawa;Katsuhito Takahashi;M. Abe;K. Hiwada;K. Ozawa;T. Murachi
Calponin, a novel homologue of troponin T, purified from chicken gizzard was found to be one of the most susceptible proteins among smooth muscle contraction‐associated proteins to hydrolysis by calpain I purified from human red blood cells. The high susceptibility of calponin was comparable to that reported for troponin T. The rate of degradation of calponin, unlike caldesmon and myosin light chain kinase, was accelerated when bound to calmodulin. When calponin existed as a bound form in both reconstituted actin filament and native thin filament, the rate of proteolysis was markedly retarded, indicating close association of calponin with actin filament. These observations are compatible with the view that calponin is an integral part of the actin‐linked contractile machinery in smooth muscle.
DOI:
--
发表时间:
1987
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Lynch,WP;Riseman,VM;Bretscher,A
通讯作者:
Bretscher,A
DOI:
--
发表时间:
1988
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Graceffa,P;Wang,CL;Stafford,WF
通讯作者:
Stafford,WF
DOI:
10.1016/0006-291x(81)91182-7
发表时间:
1981
影响因子:
3.1
作者:
Persechini,A;Mrwa,U;Hartshorne,DJ
通讯作者:
Hartshorne,DJ