Ueno H, Ooi T
J Biochem. 1977 Jun;81(6):1927-9. doi: 10.1093/oxfordjournals.jbchem.a131655.
Four fragments of alpha-tropomyosin were prepared by specific cleavage at the Cys 190 by 2-nitro-5-thiocyanobenzoic acid and by tryptic digestion. These fragments were called the N-chain corresponding to residue 1 to 189 of the original chain, the C-chain from 190 to 284, the s-fragment from 13 to 149 and/or 128, and the p-fragment from 183 to 284, respectively. Fragments individually have little binding capacity to troponin as shown by gel electrophoresis. But a new band of the complex with troponin was detected using mixtures of the fragments, one from the N-terminal side and the other from the C-terminal side, i.e., the N- and C-chains, the s- and p-fragments, the N-chain and the p-fragment, and the s-fragment and the C-chain. Therefore, the troponin binding region of tropomyosin is thought to be located between residues 150 and 190.
通过用2-硝基-5-硫氰基苯甲酸在半胱氨酸190处进行特异性切割以及胰蛋白酶消化,制备了α-原肌球蛋白的四个片段。这些片段分别被称为对应于原始链第1至189位残基的N链、第190至284位的C链、第13至149位和/或128位的s片段以及第183至284位的p片段。如凝胶电泳所示,各片段单独对肌钙蛋白的结合能力很小。但是,使用来自N端侧和C端侧的片段混合物,即N链和C链、s片段和p片段、N链和p片段以及s片段和C链,检测到了与肌钙蛋白形成的复合物的新条带。因此,原肌球蛋白的肌钙蛋白结合区域被认为位于第150至190位残基之间。