Sutoh K, Mabuchi I
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
Biochemistry. 1989 Jan 10;28(1):102-6. doi: 10.1021/bi00427a015.
A 1:1 complex of actin and depactin, an actin-depolymerizing protein isolated from starfish oocytes [Mabuchi, I. (1983) J. Cell Biol. 97, 1612-1621], was cross-linked with 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide (EDC) to introduce covalent bonds at their contact site. Locations of cross-linking sites were identified along the depactin sequence by the end-label fingerprinting, which employed site-directed antibodies against the N- and C-termini of depactin as end labels. Mappings with these end labels have revealed that the N-terminal segment of depactin (residues 1-20) contains sites in contact with the N- and C-terminal segments of actin, both of which participate in interaction with depactin [Sutoh, K., & Mabuchi, I. (1986) Biochemistry 25, 6186-6192].
肌动蛋白与去聚合蛋白（一种从海星卵母细胞中分离出的肌动蛋白解聚蛋白[马渊一，(1983)《细胞生物学杂志》97, 1612 - 1621]）形成的1:1复合物，用1 - 乙基 - 3 - [3 - (二甲氨基)丙基]碳二亚胺（EDC）进行交联，以在它们的接触位点引入共价键。通过末端标记指纹图谱沿着去聚合蛋白序列鉴定交联位点，该方法使用针对去聚合蛋白N端和C端的位点特异性抗体作为末端标记。用这些末端标记进行的图谱分析表明，去聚合蛋白的N端片段（第1 - 20位氨基酸残基）包含与肌动蛋白N端和C端片段接触的位点，这两个片段都参与与去聚合蛋白的相互作用[末藤，K.，& 马渊一，(1986)《生物化学》25, 6186 - 6192]。
