F-肌动蛋白通过赖氨酸-191和半胱氨酸-374被N，N'-对苯二马来酰亚胺进行分子间交联。
F-actin is intermolecularly crosslinked by N,N'-p-phenylenedimaleimide through lysine-191 and cysteine-374.
作者信息
Elzinga M, Phelan J J
出版信息
Proc Natl Acad Sci U S A. 1984 Nov;81(21):6599-602. doi: 10.1073/pnas.81.21.6599.
Abstract
The bifunctional reagent N,N'-p-phenylenedimaleimide (PDM) is being used in an attempt to measure distances between specific side chains in adjacent monomers within F-actin. [14C]PDM was synthesized and was used to crosslink F-actin. Uncrosslinked actin was removed by gel filtration, and, from an arginine-specific tryptic digest of the covalently crosslinked dimers and higher oligomers, one radioactive crosslinked peptide was obtained in high yield. Amino acid composition and sequence analysis indicated that it comprises residues 184-196 of one monomer and 373-375 of an adjacent actin molecule, bridged by PDM through Cys-374 and Lys-191. Thus, these groups are shown to be 1.2-1.4 nm apart in adjacent actin monomers in F-actin. This information may be crucial in establishing the orientation of actin monomers within F-actin.
摘要
双功能试剂N，N'-对苯二马来酰亚胺（PDM）正被用于尝试测量F-肌动蛋白中相邻单体特定侧链之间的距离。合成了[14C]PDM并用于交联F-肌动蛋白。通过凝胶过滤去除未交联的肌动蛋白，并且从共价交联的二聚体和更高聚体的精氨酸特异性胰蛋白酶消化物中，以高产率获得了一种放射性交联肽。氨基酸组成和序列分析表明，它包含一个单体的184-196位残基和相邻肌动蛋白分子的373-375位残基，由PDM通过Cys-374和Lys-191桥接。因此，在F-肌动蛋白的相邻肌动蛋白单体中，这些基团显示相距1.2-1.4nm。该信息对于确定F-肌动蛋白中肌动蛋白单体的取向可能至关重要。
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