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Updated: Jul 31, 2026

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
Published on: October 2, 2018
Location of disulfide bonds in antithrombin III
1Department of Medicinal Chemistry and Pharmacognosy, Purdue University, West Lafayette, Indiana 47907.
Abstract:
Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII. These results indicate that disulfide bonds join Cys 8 and Cys 128, Cys 21 and Cys 95, and Cys 247 and Cys 430. In addition, these results demonstrate that systematic searches of the amino acid sequence of a large protein for segments with molecular weights matching FAB mass spectral information is a viable method for identifying peptides independent of the specificity of the enzyme used to fragment the protein.
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