Investigation of immunological relationships among myosin light chains and troponin C.
Investigation of immunological relationships among myosin light chains and troponin C.
复制标题
肌球蛋白轻链和肌钙蛋白 C 之间免疫学关系的研究。
DOI：
10.1021/bi00639a012
复制
发表时间：
1977
期刊：
影响因子：
2.9
通讯作者：
S. Lowey
中科院分区：
文献类型：
--
作者：
L. Silberstein;S. Lowey
两类肌球蛋白轻链可以在功能上加以区分：一类是使“脱敏”的扇贝肌原纤维恢复钙调节的，另一类不是(Kendrick-Jones，J.，et al.(1976)，J.Mol.比奥尔。104、747--775)。尽管有这种功能分类，但化学分析揭示了调控轻链独有的模式，并且确实，序列比较表明两类肌球蛋白亚基之间的结构相似(Collins，J.H.(1977)，Nature(London)259,699-700；Kendrick-Jones，J.，and Jake，R.(1977)，在Tegernsee，Riecker，G.和Boehringer，Ed.，慕尼黑，西德，Springer-Verlag，pp.28-40)。使用调节轻链和非调节轻链的抗血清进行的免疫学分析表明，抗原活性与调节功能的存在或缺失之间没有相关性。然而，在肌球蛋白轻链和肌钙蛋白C之间观察到弱的交叉反应，这与基于序列同源性的建议一致，即这些亚基包含相似的结构域(Weeds，A.G.和McLachlan，A.D.(1974)，Nature(London)252,646-649)。出乎意料的是，观察到的最强的交叉反应是脊椎动物肌球蛋白碱性1和DTNB轻链之间的交叉反应。
Two classes of myosin light chains can be distinguished functionally: those that restore calcium regulation to "desensitized" scallop myofibrils, and those that do not (Kendrick-Jones, J., et al. (1976), J. Mol. Biol. 104, 747--775). Despite this functional classification, chemical analyses reveal few patterns unique to regulatory light chains, and, indeed, sequence comparisons suggest structural similarities between both classes of myosin subunits (Collins, J. H. (1977), Nature (London) 259, 699--700; Kendrick-Jones, J., and Jakes, R. (1977), in International Symposium on Myocardial Failure at Tegernsee, Riecker, G., and Boehringer, Ed., Munich, West Germany, Springer-Verlag, pp. 28--40). Immunological assays using antisera to regulatory and to nonregulatory light chains showed no correlation between antigenic activity and the presence or absence of regulatory function. Weak cross-reactivity was observed, however, among myosin light chains and troponin C, consistent with the suggestion made on the basis of sequence homologies that these subunits contain similar structural domains (Weeds, A. G., and McLachlan, A. D. (1974), Nature (London) 252, 646--649). Unexpectedly, the strongest cross-reactivity observed was that between the vertebrate myosin alkali 1 and DTNB light chains.