Preferential cleavage at aspartyl-prolyl peptide bonds in dilute acid*

Authors

  • FRANK MARCUS

    Corresponding author
    1. Department of Biological Chemistry and Structure, University of Health Sciences/The Chicago Medical School, North Chicago, IL, USA
    Search for more papers by this author

  • *

    Presented at the American Society of Biological Chemists Meeting, St. Louis, Missouri, June 1984.

  • The author would like to thank Mrs. Ida Edelstein for excellent technical assistance, Mr. Steven P. Latshaw for performing the amino acid analysis, and Dr. Robert L. Heinrikson for critical reading of the manuscript. This work was supported by National Institutes of Health Grants AM 21167 and AM 26564.

Department of Biological Chemistry and Structure University of Health Sciences/The Chicago Medical School 3333 Green Bay Road, North Chicago, IL 60064 USA

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 8–20-fold more labile in 0.015 n HCl at 100–110° 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.

Ancillary