Preferential cleavage at aspartyl-prolyl peptide bonds in dilute acid*
- 12 January 2009
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 25 (5) , 542-546
- https://doi.org/10.1111/j.1399-3011.1985.tb02208.x
Abstract
A simple, rapid technique is presented for preferential cleavage at aspartyl-prolyl peptide bonds. The method is based upon the fact that these peptide bonds are 8- to 20-fold more labile in 0.015 N HCl at 100-110.degree. than other aspartyl-X or X-aspartyl peptide bonds. The method has proven effective in the cleavage of several peptides from pig kidney fructose-1,6-bisphosphatase and should facilitate sequence analysis of proteins that contain aspartyl-prolyl linkages.Keywords
This publication has 10 references indexed in Scilit:
- Peptide mapping by polyacrylamide gel electrophoresis after cleavage at aspartyl-prolyl peptide bonds in sodium dodecyl sulfate-containing buffersAnalytical Biochemistry, 1984
- Current developments in chemical cleavage of proteinsInternational Journal of Biochemistry, 1983
- Complete amino acid sequence of pig kidney fructose-1,6-bisphosphatase.Proceedings of the National Academy of Sciences, 1982
- [15] Cleavage at aspartylprolyl bondsPublished by Elsevier ,1977
- Acidic cleavage of the aspartyl-proline bond and the limitations of the reactionAnalytical Biochemistry, 1975
- Use of fluorescamine in the chromatographic analysis of peptides from proteinsAnalytical Biochemistry, 1974
- Anomalous cleavage of aspartyl-proline peptide bonds during amino acid sequence determinationsBiochemical and Biophysical Research Communications, 1970
- [46] Partial acid hydrolysisPublished by Elsevier ,1967
- [28] Cleavage at aspartic acidPublished by Elsevier ,1967