title: Chemical cleavage of proteins in solution.
abstract: Described in this unit are five basic protocols that are widely used for specific and efficient chemical cleavage of proteins in solution. Cyanogen bromide (CNBr) cleaves at methionine (Met) residues; BNPS-skatole cleaves at tryptophan (Trp) residues; formic acid cleaves at aspartic acid-proline (Asp-Pro) peptide bonds; hydroxylamine cleaves at asparagine-glycine (Asn-Gly) peptide bonds, and 2-nitro-5-thiocyanobenzoic acid (NTCB) cleaves at cysteine (Cys) residues. Because the above loci are at relatively low abundance in most proteins, digestion with these agents will yield relatively long peptides.
authors.affiliation: Washington University School of Medicine, St. Louis, Missouri.
authors.forename: Dan L
authors.initials: DL
authors.lastname: Crimmins
authors.affiliation: Boehringer Ingelheim Pharmaceuticals, Ridgefield, Connecticut.
authors.forename: Sheenah M
authors.initials: SM
authors.lastname: Mische
authors.affiliation: University of Florida, Gainesville, Florida.
authors.forename: Nancy D
authors.initials: ND
authors.lastname: Denslow
mesh_terms: D003488:Cyanogen Bromide / Q000737:chemistry; D005561:Formates / Q000737:chemistry; D006868:Hydrolysis; D011506:Proteins / Q000737:chemistry*; D012996:Solutions; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D005561:Formates; D011506:Proteins; D012996:Solutions; C030544:formic acid; D003488:Cyanogen Bromide