Báo cáo khoa học: The calpain 1–a-actinin interaction Resting complex between the calcium-dependant protease and its target in cytoskeleton
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Calpain 1 behaviour toward cytoskeletal targets was inves-tigated using twoa-actinin isoforms from smooth and skel-etal muscles. These two isoforms which are, respectively,sensitiveandresistant tocalpaincleavage, interactwiththeprotease when usinginvitro binding assays. The stabilityof the complexes in EGTA [Kd(–Ca2+)¼0.5 ± 0.1lM]was improved in the presence of 1 mMcalcium ions[Kd(+Ca2+)¼0.05 ± 0.01lM]. Location of the bindingstructures shows that the C-terminal domain ofa-actininand each calpain subunit, 28 and 80 kDa, participates inthe interaction....
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Báo cáo khoa học: The calpain 1–a-actinin interaction Resting complex between the calcium-dependant protease and its target in cytoskeleton
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Báo cáo khoa học: The calpain 1–a-actinin interaction Resting complex between the calcium-dependant protease and its target in cytoskeleton
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