The amino acid sequence around four cysteine residues in trout actin.
Four unique carboxymethylcysteine-containing peptides were isolated from tryptic and chymotryptic digests of trout muscle actin carboxymethylated with iodo[2-(14)C]acetic acid in 6m-guanidinium chloride. The amino acid sequences of these peptides were determined and showed a high degree of homology with the corresponding sequences from rabbit actin. One of the radioactive peptides was the C-terminal peptide and another sequence probably contained the cysteine residue from the N-terminal region of the protein.
D000199:Actins / Q000032:analysis; D000595:Amino Acid Sequence; D000818:Animals; D002247:Carbon Isotopes; D002852:Chromatography, Ion Exchange; D002918:Chymotrypsin; D003545:Cysteine / Q000032:analysis*; D006146:Guanidines; D007461:Iodoacetates; D009124:Muscle Proteins / Q000032:analysis*; D010455:Peptides / Q000032:analysis / Q000302:isolation & purification; D012487:Salmonidae; D014357:Trypsin
D000199:Actins; D002247:Carbon Isotopes; D006146:Guanidines; D007461:Iodoacetates; D009124:Muscle Proteins; D010455:Peptides; D002918:Chymotrypsin; D014357:Trypsin; D003545:Cysteine