Interaction of calmodulin with skeletal muscle myosin light chain kinase.
Interaction of calmodulin with skeletal muscle myosin light chain kinase.
复制标题
钙调蛋白与骨骼肌肌球蛋白轻链激酶的相互作用。
DOI:
10.1021/bi00525a006
复制
发表时间:
1981
期刊:
影响因子:
2.9
通讯作者:
Potter,JD
中科院分区:
文献类型:
--
作者:
Crouch,TH;Holroyde,MJ;Collins,JH;Solaro,RJ;Potter,JD
1 From the Section of Contractile Proteins, Department of Pharma-cology and Cell Biophysics (THC, JHC, RJS, and JDP), and the Department of Physiology (MJH and RJS), University of Cincinnati College of Medicine, Cincinnati, Ohio 45267. Received April 20, 1981. This work was supported by National Institutes of Health Grants (HL 22619-3A, B, E) HL 22231 and AM-20875, Postdoctoral Research Training Grant HL 07382, the Muscular Dystrophy Association, and the American Heart Association (78-1167). THC is a fellow of the Muscular Dystrophy Association. JHC and RJS are holders of Research Career Development Awards. chain concentrations confirms this observation. The calcium dependence of activation of the enzyme-calmodulin complex is characterized by a Hill coefficient of 2.5, with half-activation occurring at 6.6 X1ct7 M Ca2+. The amino acid composition shows a high percentage (9.1%) of proline, which may account for the large apparentStokes radius and no clear resemblance to other skeletal muscle proteins. A comparison of the amino acid composition with that from turkey gizzard shows some resemblance. by a Ca2+-dependent myosin light chain kinase (MLCK). 1 In intact skeletal muscle, this occurs during contraction (Bárány et al., 1979) and may play a role in the posttetanic potentiation of peak twitch tension in the muscle (Manning & Stull, 1979).