کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1931248 | 1050546 | 2010 | 5 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Effects of cardiac myosin binding protein-C on the regulation of interaction of cardiac myosin with thin filament in an in vitro motility assay Effects of cardiac myosin binding protein-C on the regulation of interaction of cardiac myosin with thin filament in an in vitro motility assay](/preview/png/1931248.png)
Modulatory role of whole cardiac myosin binding protein-C (сMyBP-C) in regulation of cardiac muscle contractility was studied in the in vitro motility assay with rabbit cardiac myosin as a motor protein. The effects of cMyBP-C on the interaction of cardiac myosin with regulated thin filament were tested in both in vitro motility and ATPase assays. We demonstrate that the addition of cMyBP-C increases calcium regulated Mg-ATPase activity of cardiac myosin at submaximal calcium. The Hill coefficient for ‘pCa–velocity’ relation in the in vitro motility assay decreased and the calcium sensitivity increased when сMyBP-C was added. Results of our experiments testifies in favor of the hypothesis that сMyBP-C slows down cross-bridge kinetics when binding to actin.
Research highlights
► In the in vitro motility assay сMyBP-C interacts with thin filament and cardiac myosin.
► Cross-bridge kinetic is slowed down.
► Calcium sensitivity and the Hill coefficient of ‘pCa-velocity’ are changed.
► сMyBP-C effects on regulation of interaction of cardiac myosin with thin filament.
Journal: Biochemical and Biophysical Research Communications - Volume 401, Issue 1, 8 October 2010, Pages 159–163