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Phosphorylation by casein kinase II affects the interaction of caldesmon with smooth muscle myosin and tropomyosin.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Bogatcheva, N. V. Vorotnikov, Alexander V. Birukov, Konstantin G. Shirinsky, Vladimir P. Gusev, Nikolai B. |
| Copyright Year | 1993 |
| Abstract | Smooth muscle caldesmon was phosphorylated by casein kinase II, and the effects of phosphorylation on the interaction of caldesmon and its chymotryptic peptides with myosin and tropomyosin were investigated. The N-terminal chymotryptic peptide of caldesmon of molecular mass 27 kDa interacted with myosin. Phosphorylation of Ser-73 catalysed by casein kinase II resulted in a 2-fold decrease in the affinity of the native caldesmon (or its 27 kDa N-terminal peptide) for smooth muscle myosin. At low ionic strength, caldesmon and its N-terminal peptides of molecular masses 25 and 27 kDa were retarded on a column of immobilized tropomyosin. Phosphorylation of Ser-73 led to a 2-4-fold decrease in the affinity of caldesmon (or its N-terminal peptides) for tropomyosin. Thus phosphorylation of Ser-73 catalysed by casein kinase II affects the interaction of caldesmon with both smooth muscle myosin and tropomyosin. |
| File Format | PDF HTM / HTML |
| PubMed reference number | 8452532 |
| Journal | Medline |
| Volume Number | 290 |
| Part | 2 |
| Alternate Webpage(s) | https://istina.msu.ru/download/2833648/1gLOtN:dZd2G7dhCkMoGcm-JU0hro5NXjg/ |
| Alternate Webpage(s) | https://doi.org/10.1042/bj2900437 |
| Journal | The Biochemical journal |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
