作者: H.R. Bandi , S. Ferrari , J. Krieg , H.E. Meyer , G. Thomas
DOI: 10.1016/S0021-9258(18)53642-5
关键词: Phosphorylated Peptide 、 Protein phosphorylation 、 Ribosomal protein s6 、 Biochemistry 、 Ribosomal protein 、 Peptide 、 Molecular biology 、 Cyanogen bromide 、 Cleavage (embryo) 、 Biology 、 Phosphorylation
摘要: All of the phosphorylation sites in 40 S ribosomal protein S6 derived from serum-stimulated Swiss mouse 3T3 cells are found within a small cyanogen bromide (CNBr) peptide carboxyl terminus, Lys218-Lys249. Further cleavage CNBr or intact with endoproteinase Lys-C (endo Lys-C) generated single phosphorylated peptide, implying that all resided either between Arg231 and Lys243 Lys249 if at was blocked by nearby residue. To discern these possibilities to identify sites, purified cleaved endo Lys-C, isolated sequenced following conversion serines S-ethylcysteine. The results show extends vivo Ser235, Ser240, Ser244, Ser247.