Amino acid sequence and disulfide bond assignment of myotoxin a isolated from the venom of Prairie rattlesnake (Crotalus viridis viridis).

@article{Fox1979AminoAS,
  title={Amino acid sequence and disulfide bond assignment of myotoxin a isolated from the venom of Prairie rattlesnake (Crotalus viridis viridis).},
  author={Jay William Fox and Marshall Elzinga and Anthony T. Tu},
  journal={Biochemistry},
  year={1979},
  volume={18 4},
  pages={
          678-84
        }
}
The primary structure of myotoxin a, a myotoxin protein from the venom of the North American rattlesnake Crotalus viridis viridis, was determined and the position of the disulfide bonds assigned. The toxin was isolated, carboxymethylated, and cleaved by cyanogen bromide, and the resultant peptides were isolated. The cyanogen bromide peptides were subjected to amino acid sequence analysis. In order to assign the positions of the three disulfide bonds, the native toxin was cleaved sequentially… 
Amino acid sequence of a myotoxin from venom of the eastern diamondback rattlesnake (Crotalus adamanteus).
Automated NMR structure determination and disulfide bond identification of the myotoxin crotamine from Crotalus durissus terrificus.
Structure-function relationship of myotoxin a using peptide fragments.
New view on crotamine, a small basic polypeptide myotoxin from South American rattlesnake venom.
The nucleotide sequence of the translated and untranslated regions of a cDNA for myotoxin a from the venom of prairie rattlesnake (Crotalus viridis viridis).
TLDR
It is likely that myot toxin a is secreted as the cDNA encodes a signal peptide immediately 5' to the myotoxin a peptide code.
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