The primary structure of actin from rabbit skeletal muscle. Three cyanogen bromide peptides that are insoluble at neutral pH.
Three of the 17 peptides produced when actin is treated with cyanogen bromide are sparingly soluble at pH values near neutrality. They were separated from more soluble peptides at pH 6.0 on a column of Sephadex G-10. The soluble peptides were excluded from the gel and emerged at the void volume, while the insoluble peptides were "washed off" by the formic acid in which the sample was applied. The three insoluble peptides were sequenced as a group by studying peptides generated by tryptic and chymotryptic digestion of the mixture, and peptic digestion of the partially resolved peptides. The three peptides are: CB-15 (residues 133 to 176), CB-16 (residues 325 to 354), and CB-17 (residues 191 to 227).
D000199:Actins; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000626:Aminopeptidases; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D006863:Hydrogen-Ion Concentration; D009132:Muscles / Q000032:analysis*; D010434:Pepsin A; D010446:Peptide Fragments / Q000032:analysis; D012995:Solubility; D014357:Trypsin
D000199:Actins; D000596:Amino Acids; D010446:Peptide Fragments; D000626:Aminopeptidases; D002918:Chymotrypsin; D014357:Trypsin; D010434:Pepsin A; D003488:Cyanogen Bromide