Antibodies directed against N-terminal residues on actin do not block acto-myosin binding.
Antibodies directed against N-terminal residues on actin do not block acto-myosin binding.
复制标题
针对肌动蛋白 N 末端残基的抗体不会阻断肌动球蛋白结合。
DOI：
10.1021/bi00393a018
复制
发表时间：
1987
期刊：
影响因子：
2.9
通讯作者：
Reisler,E
中科院分区：
文献类型：
--
作者：
Miller,L;Kalnoski,M;Yunossi,Z;Bulinski,JC;Reisler,E
修订后的手稿收到1987年3月5日摘要：几项研究使用不同的方法提出了骨骼肌肌动蛋白氨基末端残基在肌动蛋白相互作用中的可能作用。为了评价Acto-S-1接触涉及肌动蛋白N端片段的意义，我们制备了针对兔骨骼肌肌动蛋白7个氨基末端残基的合成肽(AN端肽)的多克隆抗血清。从这些抗血清中制备的亲和纯化的免疫球蛋白(Ig)G(和Fab)与G-肌动蛋白和F-肌动蛋白的氨基末端都有强烈和特异的反应，但不与肌球蛋白亚段反应
Revised Manuscript Received March 5, 1987 abstract: Several studies using a variety of approaches have suggested a possible role for the amino-terminal residues of skeletal muscle actin in acto-myosin interaction. In orderto assess the significance of acto-S-1 contacts involving the N-terminal segment of actin, we have preparedpolyclonal antisera against a synthetic peptide corresponding to the seven amino-terminal residues of rabbit skeletal muscle actin (aN-terminal peptide). Affinity-purified immunoglobulin (Ig) G (and Fab) prepared from these antisera reacts strongly and specificallywith the amino-terminal segment of both G-and F-actin but not with myosin subfragment