| Literature DB >> 4019034 |
Abstract
A simple, rapid technique is presented for preferential cleavage at aspartylprolyl peptide bonds. The method is based upon the fact that these peptide bonds are 8-20-fold more labile in 0.015 N HCl at 100-110 degrees 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.Entities:
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Year: 1985 PMID： 4019034 DOI： 10.1111/j.1399-3011.1985.tb02208.x
Source DB: PubMed Journal: Int J Pept Protein Res ISSN： 0367-8377