title: Location of disulfide bonds in antithrombin III.
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.
authors.affiliation: Department of Medicinal Chemistry and Pharmacognosy, Purdue University, West Lafayette, Indiana 47907.
authors.forename: Z R
authors.initials: ZR
authors.lastname: Zhou
authors.forename: D L
authors.initials: DL
authors.lastname: Smith
mesh_terms: D000990:Antithrombin III / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D004220:Disulfides / Q000032:analysis*; D006801:Humans; D016339:Spectrometry, Mass, Fast Atom Bombardment / Q000379:methods
chemical_list: D004220:Disulfides; D000990:Antithrombin III