环磷酸腺苷依赖性蛋白激酶对兔心肌肌钙蛋白I的磷酸化位点。与肌钙蛋白C相互作用的影响。
The sites of phosphorylation of rabbit cardiac troponin I by adenosine 3':5'-cyclic monophosphate-dependent protein kinase. Effect of interaction with troponin C.
作者信息
Moir A J, Perry S V
出版信息
Biochem J. 1977 Nov 1;167(2):333-43. doi: 10.1042/bj1670333.
Abstract
- Troponin I prepared from rabbit hearts contains 1.0-1.5 mol of P/mol when isolated by affinity chromatography. Most of the covalently bound phosphate is located in residues 1-48 of the molecule. 2. 3':5'-Cyclic AMP-dependent protein kinase catalyses phosphorylation at serine-20 and serine-146. Serine-20 is more rapidly phosphorylated than serine-146. 3. In troponin I prepared from frozen hearts by affinity chromatography about 0.3-0.5 mol of P/mol is associated with serine-20 and 0.8-1.0 mol of P/mol with other site(s) in residues 1-48 of the molecule. 4. Phosphorylation at serine-20 and servine-146 is not significantly inhibited by troponin C. 5. The mechansim of the interaction of troponin C with cardiac troponin I is discussed in the light of these results.
摘要
- 通过亲和层析法从兔心脏中分离得到的肌钙蛋白I，每摩尔含有1.0 - 1.5摩尔磷。大部分共价结合的磷酸盐位于该分子的1 - 48位残基中。2. 3':5'-环磷酸腺苷依赖性蛋白激酶催化丝氨酸-20和丝氨酸-146位点的磷酸化。丝氨酸-20的磷酸化比丝氨酸-146更快。3. 通过亲和层析法从冷冻心脏中制备的肌钙蛋白I，每摩尔约有0.3 - 0.5摩尔磷与丝氨酸-20结合，每摩尔有0.8 - 1.0摩尔磷与该分子1 - 48位残基中的其他位点结合。4. 丝氨酸-20和丝氨酸-146位点的磷酸化不受肌钙蛋白C的显著抑制。5. 根据这些结果讨论了肌钙蛋白C与心肌肌钙蛋白I相互作用的机制。
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