从小鼠克隆成纤维细胞中分离和鉴定肌球蛋白。
Isolation and characterization of myosin from cloned mouse fibroblasts.
作者信息
Adelstein R S, Conti M A, Johnson G S, Pastan I, Pollard T D
出版信息
Proc Natl Acad Sci U S A. 1972 Dec;69(12):3693-7. doi: 10.1073/pnas.69.12.3693.
Myosin has been isolated from cloned mouse fibroblasts, line L-929. Fibroblast myosin: (i) binds to rabbit muscle actin and is dissociated from it by ATP, (ii) has an ATPase activity that is suppressed by Mg(2+) in 0.6 M KCl and is activated by rabbit muscle actin in the presence of Mg(2+) in 14 mM KCl, (iii) forms thin bipolar aggregates in 0.1 M KCl when viewed in the electron microscope, (iv) possesses a heavy chain with the same mobility as muscle myosin (molecular weight 200,000) in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. In these respects, fibroblast myosin appears to be similar to muscle myosin in structure and function.
肌球蛋白已从克隆的小鼠成纤维细胞系L-929中分离出来。成纤维细胞肌球蛋白：(i) 与兔肌动蛋白结合，并可被ATP从兔肌动蛋白上解离下来；(ii) 具有ATP酶活性，在0.6 M KCl中Mg(2+)可抑制该活性，而在14 mM KCl中Mg(2+)存在的情况下，兔肌动蛋白可激活该活性；(iii) 在电子显微镜下观察，在0.1 M KCl中形成薄的双极聚集体；(iv) 在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳中，其重链的迁移率与肌球蛋白相同（分子量200,000）。在这些方面，成纤维细胞肌球蛋白在结构和功能上似乎与肌球蛋白相似。
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