Abstract
There is a variety of chemical reactions known to result in the cleavage of the peptide bond. Some are nonspecific—for instance, 6M hydrochloric acid at 110°C for 24 h hydrolyzes a polypeptide to a mixture of single amino acids. Others show some discrimination, however, as to the precise nature of the amino acid residues around the bond to be broken. Some of these methods are sufficiently specific to be of use, for instance, for generating peptides for primary structure determination. These methods usefully augment those that use proteolytic enzymes (see Chapter 5), especially since they tend to act at positions occupied by less common amino acids and so generate large peptides.
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References
Fontana, A. and Gross, E. (1986) Fragmentation of Polypeptides by Chemical Methods, in Practical Protein Chemistry—A Handbook, Darbre, A., (ed.) Wiley, Chichester.
Horn, M. and Laursen, R.A. (1973) Solid-phase Edman degradation. Attachment of carboxyl-terminal homoserine peptides to an insoluble resin. FEBS Lett. 36, 285–288.
Huang, H.V., Bond, M.W., Hunkapillar, M.W., and Hood, L.E. (1983) Cleavage at tryptophanyl residues with dimethyl sulfoxide-hydrochloric acid and cyanogen bromide. Meth. Enzymol 91, 318–324.
Ingris, A.S. (1983) Cleavage at aspartic acid. Meth. Enzymol. 91, 324–332.
Wachter, E. and Werhahn, R. (1980) Cleavage of Trp-, Tyr-, and His-bonds Suited for Attachment to Amino-Supports and Subsequent Edman Degradation, in Methods in Peptide and Protein Sequence Analysis (Birr, C., ed.) Elsevier/North Holland, Amsterdam.
Landon, M. (1977) Cleavage at aspartyl-prolyl bonds. Meth. Enzymol. 47, 145–149.
Bornstein, P. and Balian, G. (1977) Cleavage at cysteine at Asn-Gly bonds with hydroxylamine. Meth. Enzymol. 47, 132–145.
Stark, G.R. (1977) Cleavage at cysteine after cyanylation. Meth. Enzymol. 47, 129–132.
Otieno, S. (1978) Generation of a free α-amino group by Raney Nickel after 2-nitro-5-thiocyanobenzoic acid cleavage at cysteine residues: Application to automated sequencing. Biochemistry 17, 5468–5474.
Ramachandran, L.K. and Witkop, B. (1976) N-Bromosuccinimide cleavage of peptides. Meth. Enzymol. 11, 283–299.
Iwai, K. and Ando, T. (1976) N → O acyl rearrangement. Meth. Enzymol. 11, 236–282.
Cohen, L.A. and Farber, L. (1967) Cleavage of tyrosyl-peptide bonds by electrolytic oxidation. Meth. Enzymol. 11, 299–308.
Fontana, A. (1972) Modification of tryptophan with BNPS-skatole (2-(2-nitrophenylsulfenyl)-3-methyl-3-bromoindolen-ine). Meth. Enzymol. 25, 419–423.
Ozols, J. and Gerard, C. (1977) Covalent structure of the membranous segment of horse cytochrome b5. Chemical cleavage of the native hemprotein. J. Biol. Chem. 252, 8549–8553.
Savige, W.E. and Fontana, A. (1977) Cleavage of the tryptophanyl peptide bond by dimethyl sulfoxide-hydrobromic acid. Meth. Enzymol. 47, 469–468.
Fontana, A., Dalzoppo, D., Grandi, C., and Zambonin, M. (1983) Cleavage at tryptophan with o-iodosobenzoic acid. Meth. Enzymol. 91, 311–318.
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© 1988 The Humana Press Inc.
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Smith, B.J. (1988). Chemical Cleavage of Proteins. In: Walker, J.M. (eds) New Protein Techniques. Methods in Molecular Biology™, vol 3. Humana Press. https://doi.org/10.1385/0-89603-126-8:71
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DOI: https://doi.org/10.1385/0-89603-126-8:71
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