Change of reactivity of lysine residues upon actin polymerization.
Change of reactivity of lysine residues upon actin polymerization.
复制标题
肌动蛋白聚合时赖氨酸残基反应性的变化。
DOI：
10.1021/bi00523a040
复制
发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Szilagyi,L
中科院分区：
文献类型：
--
作者：
Lu,RC;Szilagyi,L
Renné Chen Lu** and Laszlo Szilagyi1 abstract: The reactivity of lysine residues of actin was measured by a surface labeling method—limited reductive methylation. After labeling, actin was subjected to CNBr and enzymatic cleavage, and all lysines were obtained either singly in a peptide or as a free residue. The specific activity of each lysine was taken as the measure of its reactivity. In actin denatured in 8 M urea, the reactivity of each lysine residue is approximately equal whereasthose in G-actin fall into three categories: Lys-61 and Lys-113 are the most reactive ones; Lys-18,-213,-215,-314, and-358 are hardly reactive; the remainder, including Lys-50,-68,-84,-118,-191,-237,-283,-290,-325,-327,-335, and-372, are moderately reactive. The least reactive ones are probably buried in the native G-actin.^^. ctin is a globular protein with MT 42000, and it can exist as a monomer(G-actin) in the absence of salt or as a helical polymer (F-actin) at physiological concentration of salt. F-Actin together with tropomyosin and troponin constitutes the thin filament. It is now generally accepted that the force-generating event during muscle contraction involves an interaction between the cross bridges projecting from the myosin filaments and the thin filament and the hydrolysis of ATP. Thus, actin filaments serve as the site of cross bridge attachment and also bind the regulatory proteins tropomyosin and troponin.
