The sequences of five cyanogen bromide peptides of actin from rabbit skeletal muscle were determined, revealing that Cys-373 is the first to react with N-ethylmaleimide.
As a part of a study of the complete amino acid sequence of actin we have determined the sequences of five cyanogen bromide peptides, which together contain 158 amino acid residues, including the two ends of the molecule. The five peptides are: CB-13 (residues 1 to 44 in the intact chain), CB-11 (residues 83 to 119), CB-12 (residues 228 to 268), CB-8 (residues 283 to 298), and CB-9 (residues 355 to 374). Each of the peptides except CB-11 has one sulfhydryl group, and these peptides thus account for 4 of the 5 cysteines in actin. The reactivity of actin --SH groups toward N-ethylmaleimide was investigated, and it was found that Cys-373 (in CB-9 adjacent to the COOH-terminal phenylalanine) is the first to react with this reagent.
Elzinga et al. (Fri,) reported a other. The sequences of five cyanogen bromide peptides of actin from rabbit skeletal muscle were determined, revealing that Cys-373 is the first to react with N-ethylmaleimide.