An immunological approach to myosin light-chain function in thick filament linked regulation. 1. Characterization, specificity, and cross-reactivity of anti-scallop myosin heavy- and light-chain antibodies by competitive, solid-phase radioimmunoassay.
An immunological approach to myosin light-chain function in thick filament linked regulation. 1. Characterization, specificity, and cross-reactivity of anti-scallop myosin heavy- and light-chain antibodies by competitive, solid-phase radioimmunoassay.
复制标题
粗丝连接调节中肌球蛋白轻链功能的免疫学方法。
DOI：
10.1021/bi00508a020
复制
发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Szent-Györgyi,AG
中科院分区：
文献类型：
--
作者：
Wallimann,T;Szent-Györgyi,AG
Theo Wallimann和Andrew G. Szent-Gyorgyi* 摘要：制备了针对扇贝（Aequipecten irradians）横纹收肌肌球蛋白的调节轻链（R-LC）、“必需”轻链（SH-LC）、重链和杆状片段的特异性抗体并进行了表征。在微量滴定板上进行的竞争性固相放射免疫测定，是Kuettner等人先前描述的两种系统的组合。[Kuettner，M. G.，Wang，中国山核桃A. L.，& Nisonoff，A.（1972）J. Exp. 135，579-595]和Klinman et al. [Klinman，N. R.，Pickard，A. R.，Sigal，N. H、吉尔哈特，P. J.，Metcalf，E.美国，& Pierce，S. K.（1976）Ann. Immunol.（巴黎）127 C，489-502]，并用于不同肌球蛋白和肌球蛋白轻链的免疫学研究。抗肌球蛋白轻链抗体对同源轻链具有特异性，与异源轻链无交叉反应，即扇贝肌球蛋白的调节轻链和必需轻链可在免疫学上区分开来。这些抗体还具有高度的种属特异性。在超过30种测试的无脊椎动物或脊椎动物物种中，仅两种密切相关的软体动物物种的轻链获得部分交叉反应性。发现了两个群体的抗SH-LC抗体，其在消除扇贝肌原纤维的调节的能力上不同，并且还在肌球蛋白分子中不同，所述肌球蛋白分子由一对重链和两对不同的轻链（调节和必需轻链）组成（Lowey & Risby，1971; Weeds & Pope，1971; Burridge & Bray，1975; Kendrick-Jones等人，1976年）。肌球蛋白的基本结构组织在整个进化过程中是保守的。两条重链的α-螺旋区彼此盘绕以形成1500 A长的“尾”，另一半重链形成α-螺旋区的球状“头”区。
Theo Wallimann and Andrew G. Szent-Gyorgyi* abstract: Antibodies specific for the regulatory light-chain (R-LC),“essential” light-chain (SH-LC), heavy-chain, and rod fragment of myosin from the striated adductor muscle of scallop (Aequipecten irradians) were prepared and characterized. A competitive, solid-phase radioimmunoassay on microtiter plates, a combination of two systems described earlier by Kuettner et al.[Kuettner, M. G., Wang, A. L., & Nisonoff, A.(1972) J. Exp. Med. 135, 579-595] and Klinman et al.[Klinman, N. R., Pickard, A. R., Sigal, N. H., Gearhart, P. J., Metcalf, E. S., & Pierce, S. K.(1976) Ann. Immunol.(Paris) 127C, 489-502], was adapted and used for an immunological survey of different myosins and myosin light chains. Anti-myosin light-chain antibodies were specific for the homologous light chain and did not cross-react with the heterologous one, ie, regulatory and essential light chains of scallop myosin could be distinguished immunologically. These antibodies also had a high degree of species specificity. A partial cross-reactivity was obtained only for the light chains of two closely related molluscan species out of the over thirty invertebrate or vertebrate species tested. Two populations of anti-SH-LC antibodies were found which differed in their ability to abolish regulation of scallop myofibrils and also inIN^ Iyosin molecules consist of a pair of heavy chains and two different pairs of light chains, the regulatory and essential light chains (Lowey & Risby, 1971; Weeds & Pope, 1971; Burridge & Bray, 1975; Kendrick-Jones et al., 1976). The basic structural organization of myosin is conserved throughout evolution. The a-helical regions of the two heavy chains coil around each other to form a 1500 A long “tail”, the other half of the heavy chains forming the globular “head” regions of
登录
查看更多内容
影响因子：
5.6
作者：
BURRIDGE, K;BRAY, D
通讯作者：
BRAY, D
与调节性轻链去除相关的扇贝横纹肌张力钙控制的可逆性丧失
影响因子：
64.8
作者：
R. Simmons;A. Szent
通讯作者：
A. Szent
影响因子：
64.8
作者：
A. Weeds;B. Pope
通讯作者：
B. Pope
肌球蛋白轻链和肌钙蛋白 C 之间免疫学关系的研究。
影响因子：
2.9
作者：
L. Silberstein;S. Lowey
通讯作者：
S. Lowey
肌球蛋白轻链的物理表征。
影响因子：
2.9
作者：
W. Stafford;A. Szent
通讯作者：
A. Szent